Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Lucy L. Y. Lee"'
Publikováno v:
Biophysical Chemistry. 37:97-106
Subunit assembly plays a significant role in the regulation of rabbit muscle phosphofructokinase (PFK), although conformational changes and post-translational modifications have also been implicated to regulate the enzyme activity. In the absence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50fc03b819b5ab1511a7fd59e12306f8
https://doi.org/10.1016/0301-4622(90)88011-g
https://doi.org/10.1016/0301-4622(90)88011-g
Publikováno v:
Biophysical chemistry. 103(1)
The activity of rabbit muscle pyruvate kinase (PK) is regulated by metabolites. Besides requiring the presence of its substrates, PEP and ADP, the enzyme requires Mg ++ and K + for activity. PK is allosterically inhibited by Phe for activity. The pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02b235c01d1233fdd937ef6b1237517b
https://pubmed.ncbi.nlm.nih.gov/12504250
https://pubmed.ncbi.nlm.nih.gov/12504250
Publikováno v:
Biochemistry. 41(21)
Cyclic AMP receptor protein (CRP) regulates the expression of a large number of genes in E. coli. It is activated by cAMP binding, which leads to some yet undefined conformational changes. These changes do not involve significant redistribution of se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df059f32f4e043fcde6c48d6a8453a06
https://pubmed.ncbi.nlm.nih.gov/12022869
https://pubmed.ncbi.nlm.nih.gov/12022869
Publikováno v:
Biochemistry. 23:3813-3821
The mechanism of allosteric regulation of rabbit muscle pyruvate kinase (PK) was examined in the presence of the allosteric inhibitor phenylalanine (Phe). Steady-state kinetic, equilibrium binding, and structural studies were conducted to provide a b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1255931192cccf730bfd05df1033a959
https://doi.org/10.1021/bi00312a004
https://doi.org/10.1021/bi00312a004
Publikováno v:
Biochemistry. 19:6209-6215
The interaction of nocodazole with calf brain tubulin was studied to determine the effect of such interaction on the structure of tubulin. The effect of nocodazole on the self-association of tubulin was monitored by turbidity measurements and velocit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfcbc665c244da2ee787b8a5c52d1400
https://doi.org/10.1021/bi00567a041
https://doi.org/10.1021/bi00567a041
Publikováno v:
Journal of Biological Chemistry. 260:11060-11066
The interaction between nocodazole and calf brain tubulin in 10(-2) M sodium phosphate, 10(-4) M GTP, and 12% (v/v) dimethyl sulfoxide at pH 7.0 was studied. The number of binding sites for nocodazole was shown to be one per tubulin monomer of 50,000
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::127bd118dd73eb738dc0c799d7971f82
https://doi.org/10.1016/s0021-9258(17)39148-2
https://doi.org/10.1016/s0021-9258(17)39148-2
Autor:
James Lee, Lucy L. Y. Lee
Publikováno v:
Biochemistry. 18(24)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d86b5f23e9813901d46c82754b4f4fa
https://pubmed.ncbi.nlm.nih.gov/42431
https://pubmed.ncbi.nlm.nih.gov/42431
Autor:
James C. Lee, Lucy L. Y. Lee
Publikováno v:
Biochemistry. 26(24)
Thermal unfolding of ribonuclease, lysozyme, chymotrypsinogen, and beta-lactoglobulin was studied in the absence or presence of poly(ethylene glycols). The unfolding curves were fitted to a two-state model by a nonlinear least-squares program to obta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f75210adc7a2f0f238d245c9c9628919
https://pubmed.ncbi.nlm.nih.gov/3427106
https://pubmed.ncbi.nlm.nih.gov/3427106