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Interaction between collagen and adenosine 5′-triphosphate

✍ Scribed by B. M. Fung; Randall A. Hillson; Garland G. Lee; Arthur W. Nunnery; Reagen H. Bradford Jr.

Book ID
101717264
Publisher
Wiley (John Wiley & Sons)
Year
1976
Tongue
English
Weight
341 KB
Volume
15
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

A quantitative study was made of the adsorption of adenosine 5′‐triphosphate (ATP) on collagen by following the change in the absorbance at 258 nm of ATP in the soaking solution. The amount of ATP adsorbed decreased exponentially with the increase of pH up to pH 8 and fell off more rapidly at higher pH values. At a given pH, when the concentration of ATP was increased, the amount of ATP adsorbed increased following the pattern of a Langmuir isotherm. The adsorption was independent of the cation present. The adsorption of adenosine 5′‐diphosphate was essentially the same as that for ATP. For tendons deposited with calcium phosphate, the amount of ATP adsorbed decreased compared to natural tendons.

The adsorption of ATP on collagen fibers inhibited the contraction caused by calcium chloride, calcium bromide, and lithium bromide. In solution, ATP had very little effect on the denaturation of acid‐soluble collagen caused by calcium chloride.

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