Basement membrane collagens. Cyanogen bromide peptides of the D chain from porcine kidney
- 10 June 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (12) , 2692-2696
- https://doi.org/10.1021/bi00553a024
Abstract
An .alpha. chain size collagenous component, designated as the D chain, was isolated from the pepsin digest of porcine kidney cortices. Reduction of the D chain with 2-mercaptoethanol and carboxymethylation with iodoacetic acid resulted in the formation of two smaller components of 75,000 and 15,000 MW. The 75,000 and 15,000 MW components were separated by molecular sieve chromatography on a column of agarose A-5M. The 75,000 MW component was cleaved with CNBr in 70% formic acid. The resulting CNBr peptides were isolated by a combination of ion exchange and molecular sieve chromatography and were characterized for amino acid contents and MW. A total of 7 CNBr peptides were obtained, which together accounted for the amino acid content of the intact 75,000 MW component.This publication has 20 references indexed in Scilit:
- Nature of the Collagenous Protein in a Tumor Basement MembraneEuropean Journal of Biochemistry, 1978
- Three new α-chains of collagen from a non-basement membrane sourceBiochemical and Biophysical Research Communications, 1978
- Isolation and initial characterization of human basement membrane collagensBiochemical and Biophysical Research Communications, 1977
- Bovine renal glomerular basement membrane. Assessment of proteolysis during isolationBiochemical and Biophysical Research Communications, 1976
- Fetal membrane collagens: identification of two new collagen alpha chains.Proceedings of the National Academy of Sciences, 1976
- Isolation of three collagenous components of probable basement membrane origin from several tissuesBiochemical and Biophysical Research Communications, 1976
- Studies on the subunit composition of the renal glomerular basement membrane.Journal of Biological Chemistry, 1976
- Basement membrane procollagen is not converted to collagen in organ cultures of parietal yolk sac endoderm.Journal of Biological Chemistry, 1976
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963
- SEPARATION AND CHARACTERIZATION OF THE ALPHA-COMPONENTS AND BETA-COMPONENTS OF CALF SKIN COLLAGEN1960