Literature DB >> 237761

Content, synthesis and degradation of acetyl-coenzyme A carboxylase in the liver of growing chicks.

H Teraoka, S Numa.   

Abstract

Immunochemical techniques were used to study the mechanism underlying the marked increase in the level of acetyl-coenzyme A carboxylase activity in chick liver observed after hatching. The results of immunochemical titrations and Ouchterlony double-diffusion analysis indicated that this increase in the activity level of the enzyme was due to an elevation in the enzyme quantity. Isotopic leucine incorporation studies revealed that the rate of synthesis of the enzyme per liver was 18-fold higher in 9-day-old chicks than in 1-day-old chicks. In terms of the synthesis rate per gram of liver, this increase was 5-fold. The half-life for degradation of the enzyme in 9-day-old chicks was shown to be 46 h, whereas no apparent degradation of the enzyme as well as of total soluble liver protein was observed in 1-day-old chicks. These results indicate that the increase in the hepatic acetyl-CoA carboxylase content in growing chicks can be ascribed to accelerated synthesis of the enzyme.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 237761     DOI: 10.1111/j.1432-1033.1975.tb04087.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  1 in total

1.  Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin.

Authors:  H B White; B A Dennison; M A Della Fera; C J Whitney; J C McGuire; H W Meslar; P H Sammelwitz
Journal:  Biochem J       Date:  1976-08-01       Impact factor: 3.857

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.