The isolation and properties of bovine β-lactoglobulin C

Bell K. and McKenzie H.A. (1967) The isolation and properties of bovine β-lactoglobulin C. BBA - Protein Structure, 147 1: 109-122.

Author Bell K.
McKenzie H.A.
Title The isolation and properties of bovine β-lactoglobulin C
Journal name BBA - Protein Structure
ISSN 0005-2795
Publication date 1967-09-19
Sub-type Article (original research)
Volume 147
Issue 1
Start page 109
End page 122
Total pages 14
Subject 2700 Medicine
Abstract Methods are given for the isolation and crystallization of bovine β-lactoglobulin C. Properties of this new variant are compared with those of the A and B variants. There are differences in crystallization behaviour. The nitrogen contents and monomer molecular weights of the three variants are similar. The C variant shows little or no tendency to associate at pH 4.7 and low temperature, resembling the B variant and not the A variant. The laevorotation of C at pH 5.2 is slightly greater than that of the A or B variant but ao and bo are similar for all three variants. The ultraviolet absorption spectrum of C differs slightly from that of A or B. Optical rotatory dispersion and sedimentation studies indicate different stabilities for A, B and C and different tendencies for them to dissociate. The order of stability and dissociation are pH dependent. The three variants exhibit similar immunological behaviour.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
Versions
Version Filter Type
Citation counts: Scopus Citation Count Cited 28 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 05 Jul 2016, 12:52:20 EST by System User