Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen.

The Biochemical journal ·Vol. 191 ·No. 3 ·1980-12-01 ·Pages 873-6

Brockway BE, Forster SJ, Freedman RB

Abstract

Protein disulphide-isomerase activity was determined in homogenates of chick-embryo tissues. Activities were highest in tissues active in procollagen synthesis and were maximal at the developmental stage of maximal procollagen synthesis. These variations in protein disulphide-isomerase activity correlate closely with those previously observed for protocollagen hydroxylase activities.

MeSH Terms

Animals Bone and Bones/enzymology Cartilage/enzymology Chick Embryo Disulfides/metabolism Isomerases/metabolism Mixed Function Oxygenases/metabolism Procollagen/biosynthesis Protein Disulfide-Isomerases Tendons/enzymology Tissue Distribution

Chemicals

Disulfides Procollagen Mixed Function Oxygenases Isomerases Protein Disulfide-Isomerases

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Brockway B E

Forster S J

Freedman R B

References (14)

14 references, click to expand

Development of protocollagen proline hydroxylase activity in the chick embryo.
Biochim Biophys Acta. 1969 Oct 7;192(1):90-5 PMID: 5347975
Collagen biosynthesis during connective tissue development in chick embryo.
Dev Biol. 1972 Jul;28(3):443-53 PMID: 4339519
Developmental changes in protocollagen lysyl hydroxylase activity in the chick embryo.
Biochim Biophys Acta. 1974 Mar 20;343(1):121-8 PMID: 4857250
The biosynthesis of collagen.
Annu Rev Biochem. 1974;43(0):567-603 PMID: 4605221
Developmental changes in prolyl hydroxylase activity and protein in chick embryo.
Eur J Biochem. 1976 Jul 15;66(3):615-21 PMID: 182495
Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase.
Biochem J. 1976 Nov;159(2):377-84 PMID: 11783
The biosynthesis of procollagen.
Essays Biochem. 1976;12:77-113 PMID: 188639
Enzyme-catalysed disulphide interchange and protein biosynthesis.
Biochem Soc Trans. 1977;5(1):348-57 PMID: 330280
Protein disulphide isomerase activity in collagen-synthesising tissue of the chick embryo.
FEBS Lett. 1978 Apr 1;88(1):46-8 PMID: 639991
Biosynthesis of procollagen.
Annu Rev Biochem. 1978;47:129-62 PMID: 354493
Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition.
Eur J Biochem. 1978 Oct 16;90(3):595-603 PMID: 710449
The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen.
Eur J Biochem. 1978 Oct 16;90(3):605-13 PMID: 710450
How many distinct enzymes are responsible for the several cellular processes involving thiol:protein-disulphide interchange?
FEBS Lett. 1979 Jan 15;97(2):201-10 PMID: 33065
Prolyl 3-hydroxylase and 4-hydroxylase activities in certain rat and chick-embryo tissues and age-related changes in their activities in the rat.
Biochem J. 1979 Jan 15;178(1):127-31 PMID: 219849

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1910873

Published

1980-12-01

Pages

873-6

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1162291

Subset

External Links

PubMed source DOI: 10.1042/bj1910873 PMC Full Text View journal details

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Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen.

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