The Degradation of Collagen. III. Characterization of Soluble Products of Mild Acid Degradation

Arthur Veis; Delbert N. Eggenberger; Jerome Cohen

doi:10.1021/ja01614a004

The Degradation of Collagen. III. Characterization of Soluble Products of Mild Acid Degradation

Arthur Veis, Delbert N. Eggenberger, Jerome Cohen

Cell & Developmental Biology

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Abstract

The soluble protein obtained during the mild thermal and acid dissolution of purified bovine hide collagen which has had no previous pretreatment does not behave as a typical gelatin but is more closely related to native collagen and “procollagen.” The unfractionated soluble collagen is exceedingly polydisperse and consists of molecules ranging in molecular weight from 20 × 10⁶ to less than 1 × 10⁶. The largest fragments are highly asymmetric and have radii of gyration on the order of 6000 Å., deduced from light scattering and viscosity measurements at 40°. The soluble material obtained under a variety of conditions has been fractionated and the molecular parameters of each fraction have been determined. These parameters have been related to the initial phases of the collagen-gelatin transformation process. The stability of collagen solutions at 40° is discussed.

Original language	English (US)
Pages (from-to)	2368-2374
Number of pages	7
Journal	Journal of the American Chemical Society
Volume	77
Issue number	9
DOIs	https://doi.org/10.1021/ja01614a004
State	Published - May 1 1955

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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abstract = "The soluble protein obtained during the mild thermal and acid dissolution of purified bovine hide collagen which has had no previous pretreatment does not behave as a typical gelatin but is more closely related to native collagen and “procollagen.” The unfractionated soluble collagen is exceedingly polydisperse and consists of molecules ranging in molecular weight from 20 × 106 to less than 1 × 106. The largest fragments are highly asymmetric and have radii of gyration on the order of 6000 {\AA}., deduced from light scattering and viscosity measurements at 40°. The soluble material obtained under a variety of conditions has been fractionated and the molecular parameters of each fraction have been determined. These parameters have been related to the initial phases of the collagen-gelatin transformation process. The stability of collagen solutions at 40° is discussed.",

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Y1 - 1955/5/1

N2 - The soluble protein obtained during the mild thermal and acid dissolution of purified bovine hide collagen which has had no previous pretreatment does not behave as a typical gelatin but is more closely related to native collagen and “procollagen.” The unfractionated soluble collagen is exceedingly polydisperse and consists of molecules ranging in molecular weight from 20 × 106 to less than 1 × 106. The largest fragments are highly asymmetric and have radii of gyration on the order of 6000 Å., deduced from light scattering and viscosity measurements at 40°. The soluble material obtained under a variety of conditions has been fractionated and the molecular parameters of each fraction have been determined. These parameters have been related to the initial phases of the collagen-gelatin transformation process. The stability of collagen solutions at 40° is discussed.

AB - The soluble protein obtained during the mild thermal and acid dissolution of purified bovine hide collagen which has had no previous pretreatment does not behave as a typical gelatin but is more closely related to native collagen and “procollagen.” The unfractionated soluble collagen is exceedingly polydisperse and consists of molecules ranging in molecular weight from 20 × 106 to less than 1 × 106. The largest fragments are highly asymmetric and have radii of gyration on the order of 6000 Å., deduced from light scattering and viscosity measurements at 40°. The soluble material obtained under a variety of conditions has been fractionated and the molecular parameters of each fraction have been determined. These parameters have been related to the initial phases of the collagen-gelatin transformation process. The stability of collagen solutions at 40° is discussed.

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The Degradation of Collagen. III. Characterization of Soluble Products of Mild Acid Degradation

Abstract

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