Titlebook: Enzyme Induction and Modulation; V. A. Najjar Book 1983 Martinus Nijhoff Publishers, Boston 1983 Coenzym.Glutamin.Nucleotide.RNA.biochemis

衍生

Function and induction of the microsomal heme oxygenaseiological heme catabolism to yield biliverdin in animals. Heme oxygenase purified from either pig spleen or rat liver has a minimum molecular weight of 32 000, and binds heme to form a 1:1 complex which exhibits properties resembled to those of hemoglobin and myoglobin. Heme degradation in the heme

Lamina

propose

Modulation of poly(A)(+)mRNA-metabolizing and transporting systems under special consideration of mindoribonucleaselV and2‘,3’-exoribonuclease. Moreover, poly(A)-associated proteins as well as the cytoskeletal proteins actin and tubulin have been found to be involved in poly(A) metabolism of mRNA; their modulation effects on poly(A) metabolizing enzyme systems will be described in greater detail.

Accord

Messenger RNA for glutamine synthetaseids in the embryonic chick retina represents one of the systems most extensively studied. GS mRNA was first identified at the polysomal level by immunochemical precipitation of fractionated polysomes containing nascent GS chains with anti-GS γ-globulin. The mRNA has been shown to be polyadenylated a

meritorious

有毒

PATHY

Regulation of expression of genes for enzymes of the mammalian urea cycle in permanent cell-culture e rat-hepatoma lines, we have characterized extensively in one (H4-II-E-C3) the mode of action of glucocorticoids in augmenting the cellular levels of this enzyme as well as of argininosuccinate synthetase. To this end, we have recently demonstrated that these stimulations are both mediated by bindi

evanescent

Plasma protein induction by isolated hepatocyteson factors, etc.) isolated from hepatocytes. Studies on fetal or embryonic hepatocytes and hepatomas are yielding information on the regulation of secretory protein synthesis during development and following neoplastic transformation.

保守

Function and induction of the microsomal heme oxygenase number of non-heme substances including insulin, epinephrine, endotoxin, carbon disulfide, certain metal ions, diethylmaleate, bromobenzene, chlorinated benzenes, and interferon- inducing agents, and some of those non-heme substances appear to induce heme oxygenase independently of the mediation by

BIAS