ioscan system 200 imaging scanner (BIOSCAN INC)
90
Structured Review
BIOSCAN INC
ioscan system 200 imaging scanner
Ioscan System 200 Imaging Scanner, supplied by BIOSCAN INC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ioscan+system+200+imaging+scanner/ioscan+system+200+imaging+scanner/pm10415125-100-9-15
Average 90 stars, based on 1 article reviews
Ioscan System 200 Imaging Scanner, supplied by BIOSCAN INC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ioscan+system+200+imaging+scanner/ioscan+system+200+imaging+scanner/pm10415125-100-9-15
Average 90 stars, based on 1 article reviews
ioscan system 200 imaging scanner - by Bioz Stars,
2026-09
90/100 stars
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Thin Layer Chromatography:Article Title: Identification of specific residues involved in substrate discrimination in two plant O-methyltransferases. Article Snippet: O O c m Among the large number of plant O-methyltranserases that are involved in secondary metabolism, nly a few have been enzymatically characterized, nd little information is available on the structure of heir substrate binding site and the mechanism which etermines their substrate specificity and methylaion regiospecificity.. We have previously reported the solation of two O-methyltransferases, S-adenosyl-Lethionine:(iso)eugenol O-methyltransferase (IEMT) nd S-adenosyl-L-methionine:caffeic acid O-methylransferase (COMT) from Clarkia breweri, an annual lant from California.. While IEMT and COMT (which ethylate eugenol/isoeugenol and caffeic acid/5ydroxyferulic acid, respectively) share 83% identity t the amino acid level, they have distinct substrate pecificity and methylation regiospecificity. Imaging:Article Title: Identification of specific residues involved in substrate discrimination in two plant O-methyltransferases. Article Snippet: O O c m Among the large number of plant O-methyltranserases that are involved in secondary metabolism, nly a few have been enzymatically characterized, nd little information is available on the structure of heir substrate binding site and the mechanism which etermines their substrate specificity and methylaion regiospecificity.. We have previously reported the solation of two O-methyltransferases, S-adenosyl-Lethionine:(iso)eugenol O-methyltransferase (IEMT) nd S-adenosyl-L-methionine:caffeic acid O-methylransferase (COMT) from Clarkia breweri, an annual lant from California.. While IEMT and COMT (which ethylate eugenol/isoeugenol and caffeic acid/5ydroxyferulic acid, respectively) share 83% identity t the amino acid level, they have distinct substrate pecificity and methylation regiospecificity. |