Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Barbara A. Castellani"'
Publikováno v:
Journal of Biological Chemistry. 242:4395-4401
The fragmentation of human serum albumin by trypsin was studied by electrophoresis and by gel filtration. Brief hydrolysis at pH 8.5 yields a characteristic pattern of fragmentation, the most conspicuous feature of which is the appearance of a 51,000
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b3a8a7d31ba54a4d4446e567a531d9e
https://doi.org/10.1016/s0021-9258(18)99552-9
https://doi.org/10.1016/s0021-9258(18)99552-9
Publikováno v:
Journal of Biological Chemistry. 243:4070-4076
The rate of formation of ribonuclease-S from ribonuclease A by the action of subtilisin was measured at pH 5.5 in the presence and absence of the strongly bound ribonuclease inhibitor, 2′-cytidylate. Presence of the inhibitor in the active center s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40aca9a489a5af8d781922c2012d543c
https://doi.org/10.1016/s0021-9258(18)93280-1
https://doi.org/10.1016/s0021-9258(18)93280-1
Publikováno v:
Journal of Biological Chemistry. 242:4402-4408
Interaction of human serum albumin with anionic azo dyes decreases the susceptibility of the former to hydrolytic attack by five different proteases. By using methyl orange as the ligand, it is shown that the occupation of the two strong binding site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e12ea630d01736f84cc4b77a147ca170
https://doi.org/10.1016/s0021-9258(18)99553-0
https://doi.org/10.1016/s0021-9258(18)99553-0