Zobrazeno 1 - 5
of 5
pro vyhledávání: '"David K. McClintock"'
Autor:
Jay E. Birnbaum, Benjamin M. Sparano, David K. McClintock, Edward L. Tolman, Adolph E. Sloboda
Publikováno v:
Pharmacology. 25:27-38
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0317f65dd3581b8e20882da6a200fded
https://doi.org/10.1159/000137775
https://doi.org/10.1159/000137775
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
Autor:
David K. McClintock, Gabor Markus
Publikováno v:
Journal of Biological Chemistry. 243:2855-2862
Evidence is presented for the existence of several ligand-stabilized forms of aspartate transcarbamylase, as identified by their susceptibilities to proteolysis. The rate of tryptic digestion of the enzyme is significantly increased when the substrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf7b8bcdf318c0a335006068258323f2
https://doi.org/10.1016/s0021-9258(18)93350-8
https://doi.org/10.1016/s0021-9258(18)93350-8
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
Publikováno v:
Journal of Biological Chemistry. 246:762-771
Evidence concerning conformational changes in aspartate transcarbamylase of Escherichia coli is reviewed in order to evaluate the level of structural organization at which the changes relevant to allosteric behavior take place, and to assess the cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::533da2a72d716f449e4f855c32381dde
https://doi.org/10.1016/s0021-9258(18)62476-7
https://doi.org/10.1016/s0021-9258(18)62476-7