FUNCTIONAL-CHANGES IN BETA-LACTOGLOBULIN BY CONJUGATION WITH CARBOXYMETHYL DEXTRAN

被引:80
作者
HATTORI, M [1 ]
NAGASAWA, K [1 ]
AMETANI, A [1 ]
KAMINOGAWA, S [1 ]
TAKAHASHI, K [1 ]
机构
[1] UNIV TOKYO, DEPT AGR CHEM, TOKYO 113, JAPAN
关键词
BETA-LACTOGLOBULIN; NEOGLYCOCONJUGATE; FUNCTIONAL IMPROVEMENT; ACIDIC POLYSACCHARIDE; PROTEIN CONJUGATION; EMULSIFICATION; RETINOL BINDING; LIPOCALIN;
D O I
10.1021/jf00046a009
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Two bovine beta-lactoglobulin-carboxymethyl dextran (beta-LG-CMD) conjugates (conjugates 10A and 10B) were prepared to improve the protein function by using water-soluble carbodiimide. The molar ratios of beta-LG to CMD in the conjugates (Conj) were 7:2 (Conj 10A) and 1:1 (Conj 10B). The isoelectric point of each conjugate was 4.7-4.8, which is lower than that of beta-LG. Spectroscopic studies suggested that the conformation around had not changed in either conjugate but the alpha-helix content of Conj 10A had markedly decreased as compared with that of beta-LG. Structural analyses with monoclonal antibodies indicated the conformational change of 125Thr-135Lys (a-helix) in Conj 10A and of 15Val-29Ile (beta-sheet) in Conj 10B. The denaturation temperature of each conjugate was about 89 degrees C, which is much higher than that of native beta-LG, Each conjugate maintained retinol binding activity as strong as that of native beta-LG. The emulsifying activity of beta-LG at neutral pH was much improved by conjugation with CMD.
引用
收藏
页码:2120 / 2125
页数:6
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