The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation

A. Veis; R. S. Bhatnagar; C. A. Shuttleworth; S. Mussell

doi:10.1016/0005-2795(70)90048-6

The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation

A. Veis^*, R. S. Bhatnagar, C. A. Shuttleworth, S. Mussell

^*Corresponding author for this work

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

29 Scopus citations

Abstract

Insoluble bovine corium collagen was dissolved in acid following a lyotropic swelling step at 25° and neutral pH at low ionic strength. The lyotropic swelling apparently relaxes interfibrillar bonding and permits the fibrils to swell without limit in acetic acid. Yields of soluble collagen were on the order of 20% of the total. The use of purified amylase or chelating agents did not increase the yields. Electron microscopic examination and intrinsic viscosity determination showed the soluble collagen to be present as very long thin filaments. CM-cellulose chromatography and disc electrophoresis of the denatured collagen indicated that the solubilized collagen was very highly cross-linked. These data support the concept of the limiting microfibrillar structure of collagen fibers and indicate that one main cross-linking system is entirely internal to the microfibrils.

Original language	English (US)
Pages (from-to)	97-112
Number of pages	16
Journal	BBA - Protein Structure
Volume	200
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(70)90048-6
State	Published - Jan 20 1970
Externally published	Yes

Funding

This work is supported by Grants from U.S. Department of Agriculture (No. 12-14-1oo-8933(73)) and the National Institute of Health GM o8222.

ASJC Scopus subject areas

General Medicine

Access to Document

10.1016/0005-2795(70)90048-6

Cite this

@article{265abb6e007147a89bba74b3dd3b4d32,

title = "The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation",

abstract = "Insoluble bovine corium collagen was dissolved in acid following a lyotropic swelling step at 25° and neutral pH at low ionic strength. The lyotropic swelling apparently relaxes interfibrillar bonding and permits the fibrils to swell without limit in acetic acid. Yields of soluble collagen were on the order of 20% of the total. The use of purified amylase or chelating agents did not increase the yields. Electron microscopic examination and intrinsic viscosity determination showed the soluble collagen to be present as very long thin filaments. CM-cellulose chromatography and disc electrophoresis of the denatured collagen indicated that the solubilized collagen was very highly cross-linked. These data support the concept of the limiting microfibrillar structure of collagen fibers and indicate that one main cross-linking system is entirely internal to the microfibrils.",

author = "A. Veis and Bhatnagar, {R. S.} and Shuttleworth, {C. A.} and S. Mussell",

note = "Funding Information: This work is supported by Grants from U.S. Department of Agriculture (No. 12-14-1oo-8933(73)) and the National Institute of Health GM o8222.",

year = "1970",

month = jan,

day = "20",

doi = "10.1016/0005-2795(70)90048-6",

language = "English (US)",

volume = "200",

pages = "97--112",

journal = "BBA - Protein Structure",

issn = "0005-2795",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation

AU - Veis, A.

AU - Bhatnagar, R. S.

AU - Shuttleworth, C. A.

AU - Mussell, S.

N1 - Funding Information: This work is supported by Grants from U.S. Department of Agriculture (No. 12-14-1oo-8933(73)) and the National Institute of Health GM o8222.

PY - 1970/1/20

Y1 - 1970/1/20

N2 - Insoluble bovine corium collagen was dissolved in acid following a lyotropic swelling step at 25° and neutral pH at low ionic strength. The lyotropic swelling apparently relaxes interfibrillar bonding and permits the fibrils to swell without limit in acetic acid. Yields of soluble collagen were on the order of 20% of the total. The use of purified amylase or chelating agents did not increase the yields. Electron microscopic examination and intrinsic viscosity determination showed the soluble collagen to be present as very long thin filaments. CM-cellulose chromatography and disc electrophoresis of the denatured collagen indicated that the solubilized collagen was very highly cross-linked. These data support the concept of the limiting microfibrillar structure of collagen fibers and indicate that one main cross-linking system is entirely internal to the microfibrils.

AB - Insoluble bovine corium collagen was dissolved in acid following a lyotropic swelling step at 25° and neutral pH at low ionic strength. The lyotropic swelling apparently relaxes interfibrillar bonding and permits the fibrils to swell without limit in acetic acid. Yields of soluble collagen were on the order of 20% of the total. The use of purified amylase or chelating agents did not increase the yields. Electron microscopic examination and intrinsic viscosity determination showed the soluble collagen to be present as very long thin filaments. CM-cellulose chromatography and disc electrophoresis of the denatured collagen indicated that the solubilized collagen was very highly cross-linked. These data support the concept of the limiting microfibrillar structure of collagen fibers and indicate that one main cross-linking system is entirely internal to the microfibrils.

UR - http://www.scopus.com/inward/record.url?scp=0014955669&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014955669&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(70)90048-6

DO - 10.1016/0005-2795(70)90048-6

M3 - Article

C2 - 4983330

AN - SCOPUS:0014955669

SN - 0005-2795

VL - 200

SP - 97

EP - 112

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 1

ER -

The solubilization of mature, polymeric collagen fibrils by lyotropic relaxation

Abstract

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this