Effect of monovalent anions on type I collagen fibrillogenesis in vitro

Effect of monovalent anions on type I collagen fibrillogenesis in vitro

The effect of a set of monovalent anions with different preferential binding to proteins (C1 −, Br −, I −, SCN −) on the kinetics of type I collagen fibrillogenesis was studied. Evidences obtained from turbidity-time curves and the Arrenhius plot suggested the presence of a conformational change pri...

Full description

Saved in:
Bibliographic Details
Published in:International journal of biological macromolecules Vol. 19; no. 1; pp. 15 - 20
Main Authors: Delorenzi, Nestor J., Sculsky, Guillermina, Gatti, Carlos A.
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 01-07-1996
Subjects:
Anions - pharmacology
Bromides - pharmacology
Chlorides - pharmacology
Collagen - chemical synthesis
Collagen - physiology
Collagen type I
Fibrillogenesis
Hofmeister series
Iodides - pharmacology
Monovalent anions
Nephelometry and Turbidimetry
Protein Conformation - drug effects
Thiocyanates - pharmacology
Time Factors
Fibrillogenesis
Collagen type I
Monovalent anions
Hofmeister series
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The effect of a set of monovalent anions with different preferential binding to proteins (C1 −, Br −, I −, SCN −) on the kinetics of type I collagen fibrillogenesis was studied. Evidences obtained from turbidity-time curves and the Arrenhius plot suggested the presence of a conformational change prior to fibril formation, also supported by previous data available in the literature. A model of the initial steps of collagen assembly was proposed that could explain the action of the monovalent anions studied and other cosolvents on fibrillogenesis. Analysis of fibril width and 1-anilinonaphthalene-8-sulfonic acid (ANS) binding to collagen pointed to the presence of a nucleation process within the lag time
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0141-8130
1879-0003
DOI:10.1016/0141-8130(96)01094-X