ribonuclease b  (New England Biolabs)


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    New England Biolabs ribonuclease b
    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of <t>RNase</t> <t>B</t> (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).
    Ribonuclease B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    ribonuclease b - by Bioz Stars, 2023-01
    94/100 stars

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    1) Product Images from "Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples"

    Article Title: Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples

    Journal: ACS Omega

    doi: 10.1021/acsomega.2c05429

    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).
    Figure Legend Snippet: (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).

    Techniques Used:

    ribonuclease b  (New England Biolabs)


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    Structured Review

    New England Biolabs ribonuclease b
    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of <t>RNase</t> <t>B</t> (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).
    Ribonuclease B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ribonuclease b/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ribonuclease b - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples"

    Article Title: Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples

    Journal: ACS Omega

    doi: 10.1021/acsomega.2c05429

    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).
    Figure Legend Snippet: (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).

    Techniques Used:

    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    Processing of HM-type N -glycans on RNAse B. Mass spectrometry of <t>RNAse</t> <t>B</t> treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Mechanism of cooperative N -glycan processing by the multi-modular endoglycosidase EndoE"

    Article Title: Mechanism of cooperative N -glycan processing by the multi-modular endoglycosidase EndoE

    Journal: Nature Communications

    doi: 10.1038/s41467-022-28722-w

    Processing of HM-type N -glycans on RNAse B. Mass spectrometry of RNAse B treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .
    Figure Legend Snippet: Processing of HM-type N -glycans on RNAse B. Mass spectrometry of RNAse B treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .

    Techniques Used: Mass Spectrometry, Negative Control, Positive Control, Software

    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94/100 stars

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    bovine rnase b  (New England Biolabs)


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    New England Biolabs bovine rnase b
    Experimental conditions for optimal limited deglycosylation of bovine <t>RNase</t> <t>B</t> and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Bovine Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bovine rnase b/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
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    bovine rnase b - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay"

    Article Title: Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay

    Journal: bioRxiv

    doi: 10.1101/2021.06.04.447131

    Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Figure Legend Snippet: Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.

    Techniques Used: Concentration Assay, Migration, SDS Page

    rnase b  (New England Biolabs)


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    Structured Review

    New England Biolabs rnase b
    Experimental conditions for optimal limited deglycosylation of bovine <t>RNase</t> <t>B</t> and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase b/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase b - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay"

    Article Title: Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay

    Journal: bioRxiv

    doi: 10.1101/2021.06.04.447131

    Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Figure Legend Snippet: Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.

    Techniques Used: Concentration Assay, Migration, SDS Page

    ribonuclease b  (New England Biolabs)


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    New England Biolabs ribonuclease b
    Ribonuclease B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase b/product/New England Biolabs
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    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase b/product/New England Biolabs
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    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or <t>RNase</t> <t>B</t>
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "New Enzymatic Approach to Distinguish Fucosylation Isomers of N‑Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry"

    Article Title: New Enzymatic Approach to Distinguish Fucosylation Isomers of N‑Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry

    Journal: Journal of proteome research

    doi: 10.1021/acs.jproteome.0c00024

    SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or RNase B
    Figure Legend Snippet: SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or RNase B

    Techniques Used: SDS Page

    rnase b  (New England Biolabs)


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    New England Biolabs rnase b
    SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or <t>RNase</t> <t>B</t>
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "New Enzymatic Approach to Distinguish Fucosylation Isomers of N‑Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry"

    Article Title: New Enzymatic Approach to Distinguish Fucosylation Isomers of N‑Linked Glycans in Tissues Using MALDI Imaging Mass Spectrometry

    Journal: Journal of proteome research

    doi: 10.1021/acs.jproteome.0c00024

    SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or RNase B
    Figure Legend Snippet: SDS-PAGE analysis of N-linked glycans cleaved by PNGase F or Endo F3. (A) Cartoon description of Endo F3 vs PNGase F cleavage on core-fucosylated N-linked glycans. For glycans, red triangles represent fucose, blue squares represent N-acetylglucosamine, green circles represent mannose, and yellow circles represent galactose. (B) SDS-PAGE analysis of Endo F3 and PNGase F digestion of human Fetuin-A or RNase B

    Techniques Used: SDS Page

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    New England Biolabs ribonuclease b
    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of <t>RNase</t> <t>B</t> (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).
    Ribonuclease B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ribonuclease b/product/New England Biolabs
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    New England Biolabs rnase b
    Processing of HM-type N -glycans on RNAse B. Mass spectrometry of <t>RNAse</t> <t>B</t> treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .
    Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs bovine rnase b
    Experimental conditions for optimal limited deglycosylation of bovine <t>RNase</t> <t>B</t> and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.
    Bovine Rnase B, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).

    Journal: ACS Omega

    Article Title: Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples

    doi: 10.1021/acsomega.2c05429

    Figure Lengend Snippet: (a) 0,2 A, 2,4 A, and B type ISD fragment position of N -glycans. MALDI–ISD spectrum of RNase B (20 pmol μL –1 ) with (b) 1,5-diaminonaphthalene (DAN)/DHB/Na (12:10:1), (c) DAN/aniline/DHB/Na (2:10:10:1), and (d) DAN/DHB/Na (2:10:1).

    Article Snippet: Ribonuclease B (RNase B) from bovine was purchased from New England BioLabs, Inc. (Beverly, MA, USA).

    Techniques:

    Processing of HM-type N -glycans on RNAse B. Mass spectrometry of RNAse B treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .

    Journal: Nature Communications

    Article Title: Mechanism of cooperative N -glycan processing by the multi-modular endoglycosidase EndoE

    doi: 10.1038/s41467-022-28722-w

    Figure Lengend Snippet: Processing of HM-type N -glycans on RNAse B. Mass spectrometry of RNAse B treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18L E186Q d EndoE-GH18L + EndoE-GH18L E186Q e EndoE-GH20 f EndoE-GH20 E662Q g EndoE-GH20 + EndoE-GH20 E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoE E186Q l EndoE E186Q + EndoE-GH18L m EndoE E662Q n EndoE E662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table .

    Article Snippet: For the LC-MS enzymatic activity assays, 20 µL reactions were setup containing 1 µM of RNAse B (NEB), Rituximab ± BgaA galactosidase or human transferrin (Sigma–Aldrich)± MvNA sialidase±BgaA galactosidase and 1 µM of enzyme in PBS pH 7.4.

    Techniques: Mass Spectrometry, Negative Control, Positive Control, Software

    Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.

    Journal: bioRxiv

    Article Title: Systems-wide analysis of glycoprotein conformational changes by limited deglycosylation assay

    doi: 10.1101/2021.06.04.447131

    Figure Lengend Snippet: Experimental conditions for optimal limited deglycosylation of bovine RNase B and fetuin by PNGase F were determined. The optimal A ) NP-40 concentration, B ) temperature, C ) and D ) PNGase F:glycoprotein ratio for RNase B and fetuin, respectively, and, E ) and F ) the optimal time for the deglycosylation of RNase B and fetuin, respectively, were assayed by differential migration of the glycoproteins in 15% SDS-PAGE. Fully deglycosylated (+) and fully glycosylated (−) proteins were included for each optimization reaction, denoted by FD and FG, respectively.

    Article Snippet: Proof-of-concept and optimization of the LDA method were performed using two standard glycoproteins, bovine RNase B and fetuin (New England Biolabs) by PNGase F (New England Biolabs) under native conditions.

    Techniques: Concentration Assay, Migration, SDS Page