The isolation of a soluble type III collagen precursor from rat skin

Joan Anesey; Paul G. Scott; Arthur Veis; Douglas Chyatte

doi:10.1016/0006-291X(75)90414-3

The isolation of a soluble type III collagen precursor from rat skin

Joan Anesey^*, Paul G. Scott, Arthur Veis, Douglas Chyatte

^*Corresponding author for this work

Cell & Developmental Biology

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

A soluble form of type III collagen has been isolated from the 1.0 M NaCl neutral salt soluble extract of rat skin. This component has a molecular weight of 350,000 and is converted by reduction and alkylation to three identical α-chains with molecular weight 118,000. Segment-long-spacing precipitates produced from the renatured disulfide-linked component are about 300 Å longer than collagen with extensions at both the amino and carboxyl terminal ends. Pepsin treatment removes both amino and carboxyl terminal extensions. These and radioisotope incorporation data lead to the conclusion that this component is a precursor of the [αl(III)₃] collagen.

Original language	English (US)
Pages (from-to)	946-952
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	62
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(75)90414-3
State	Published - Feb 17 1975

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(75)90414-3

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title = "The isolation of a soluble type III collagen precursor from rat skin",

abstract = "A soluble form of type III collagen has been isolated from the 1.0 M NaCl neutral salt soluble extract of rat skin. This component has a molecular weight of 350,000 and is converted by reduction and alkylation to three identical α-chains with molecular weight 118,000. Segment-long-spacing precipitates produced from the renatured disulfide-linked component are about 300 {\AA} longer than collagen with extensions at both the amino and carboxyl terminal ends. Pepsin treatment removes both amino and carboxyl terminal extensions. These and radioisotope incorporation data lead to the conclusion that this component is a precursor of the [αl(III)3] collagen.",

author = "Joan Anesey and Scott, {Paul G.} and Arthur Veis and Douglas Chyatte",

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T1 - The isolation of a soluble type III collagen precursor from rat skin

AU - Anesey, Joan

AU - Scott, Paul G.

AU - Veis, Arthur

AU - Chyatte, Douglas

PY - 1975/2/17

Y1 - 1975/2/17

N2 - A soluble form of type III collagen has been isolated from the 1.0 M NaCl neutral salt soluble extract of rat skin. This component has a molecular weight of 350,000 and is converted by reduction and alkylation to three identical α-chains with molecular weight 118,000. Segment-long-spacing precipitates produced from the renatured disulfide-linked component are about 300 Å longer than collagen with extensions at both the amino and carboxyl terminal ends. Pepsin treatment removes both amino and carboxyl terminal extensions. These and radioisotope incorporation data lead to the conclusion that this component is a precursor of the [αl(III)3] collagen.

AB - A soluble form of type III collagen has been isolated from the 1.0 M NaCl neutral salt soluble extract of rat skin. This component has a molecular weight of 350,000 and is converted by reduction and alkylation to three identical α-chains with molecular weight 118,000. Segment-long-spacing precipitates produced from the renatured disulfide-linked component are about 300 Å longer than collagen with extensions at both the amino and carboxyl terminal ends. Pepsin treatment removes both amino and carboxyl terminal extensions. These and radioisotope incorporation data lead to the conclusion that this component is a precursor of the [αl(III)3] collagen.

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AN - SCOPUS:0016663438

SN - 0006-291X

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SP - 946

EP - 952

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The isolation of a soluble type III collagen precursor from rat skin

Abstract

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