Adentitious 发表于 2025-3-21 18:16:50

书目名称Metabolic Interconversion of Enzymes影响因子(影响力)<br>        http://figure.impactfactor.cn/if/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes影响因子(影响力)学科排名<br>        http://figure.impactfactor.cn/ifr/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes网络公开度<br>        http://figure.impactfactor.cn/at/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes网络公开度学科排名<br>        http://figure.impactfactor.cn/atr/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes被引频次<br>        http://figure.impactfactor.cn/tc/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes被引频次学科排名<br>        http://figure.impactfactor.cn/tcr/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes年度引用<br>        http://figure.impactfactor.cn/ii/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes年度引用学科排名<br>        http://figure.impactfactor.cn/iir/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes读者反馈<br>        http://figure.impactfactor.cn/5y/?ISSN=BK0631243<br><br>        <br><br>书目名称Metabolic Interconversion of Enzymes读者反馈学科排名<br>        http://figure.impactfactor.cn/5yr/?ISSN=BK0631243<br><br>        <br><br>

提升 发表于 2025-3-21 22:38:22

Electron Microscopy of Muscle Phosphorylases , and ,,ylase . in solution is a tetramer of molecular weight 400000 (s=13,2S), and phosphorylase . is a dimer of molecular weight 200000 (1). In the presence of p-chlormercuribenzoate (2) phosphorylases . and . dissociate into four and two monomers, respectively, both having the same molecular weight. On c

责难 发表于 2025-3-22 04:17:54

Discussion,GDP is a phosphorylatable agent? My second point concerns the pH-dependency of the reversal of your reaction. We have found reversal of the adenyl-transferase reaction in glutamine synthetase by strongly pH dependent pyrophosphorylation. The equilibrium constant at pH 6 is about 1, at pH 7 it is 10,

Herpetologist 发表于 2025-3-22 06:01:05

Studies on Glycogen Phosphorylase in Solution and in the Crystalline State,ε-amino group of lysine. In order to explain the absorbance of the bound pyridoxal-P at about 330 nm, these authors suggested that another group (called X) added to the original Schiff base formed between the ε-amino and the aldehyde. This group X is still unknown but it should be nucleophilic and a

agglomerate 发表于 2025-3-22 11:59:49

Association-dissociation Properties of NaBH,-reduced Phosphorylase ,, The enzyme exists as dimers and tetramers, and it has been shown that both phosphorylase . and . undergo dissociation-association reactions which affect enzymic activity (3,4). The formation of the monomer was first demonstrated by Madsen and Cori (5) by reaction of phosphorylase with PMB. Other me

Spongy-Bone 发表于 2025-3-22 16:01:28

The Mechanism of Action of Cyclic AMP in the Activation of Phosphorylase Kinase,se kinase, has very little activity at pH 6.8 and is only partially active at higher pH values. The other form of the enzyme, activated phosphorylase kinase, is highly active at pH 6.8 and at pH 8.2. Conversion of nonactivated phosphorylase kinase to the activated form can be brought about .. by lim

Cpap155 发表于 2025-3-22 20:39:48

http://reply.papertrans.cn/64/6313/631243/631243_7.png

Cloudburst 发表于 2025-3-22 22:05:46

http://reply.papertrans.cn/64/6313/631243/631243_8.png

Anonymous 发表于 2025-3-23 05:19:00

Properties of Purified Glycogen Synthetase , from Liver,2 major peaks of synthetase . activity were found in the absence of ligands, plus small amounts of higher molecular weight components. The heavier peak appeared to be a dimer of the lighter peak and was of approximately 258, 000 to 284, 000 molecular weight. In the presence of ligands a single, near

negligence 发表于 2025-3-23 06:18:34

http://reply.papertrans.cn/64/6313/631243/631243_10.png
页: [1] 2 3 4 5 6
查看完整版本: Titlebook: Metabolic Interconversion of Enzymes; O. Wieland,E. Helmreich,H. Holzer Book 1972 Springer-Verlag Berlin Heidelberg 1972 Enzym.Enzyme.Stof