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固定化胰蛋白酶对β-酪蛋白的模型蛋白水解作用。

Model proteolysis of beta-casein by immobilized trypsin.

作者信息

Reimerdes E H

出版信息

J Dairy Res. 1979 Apr;46(2):223-6. doi: 10.1017/s0022029900017088.

DOI:10.1017/s0022029900017088
PMID:469047
Abstract

The enzymic degradation of beta-casein by immobilized trypsin is described and its use as a model system to study proteolytic reactions which occur in milk during processing is examined. Quantitative determination of proteolysis can be obtained by densitometric transmission measurement of patterns obtained by polyacrylamide-gel electrophoresis. Staining properties of some of the individual components in the electrophoretic patterns were determined by calibration with pure protein and peptide preparations. The isolation of pure beta- and gamma-caseins and the preparation of several forms of immobilized trypsin are outlined.

摘要

本文描述了固定化胰蛋白酶对β-酪蛋白的酶促降解,并研究了其作为模型系统用于研究牛奶加工过程中发生的蛋白水解反应。通过对聚丙烯酰胺凝胶电泳所得图谱进行光密度透射测量,可以对蛋白水解进行定量测定。通过用纯蛋白质和肽制剂进行校准,确定了电泳图谱中一些单个成分的染色特性。概述了纯β-酪蛋白和γ-酪蛋白的分离以及几种固定化胰蛋白酶形式的制备。

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引用本文的文献

1
Characterization of trypsin immobilized on oxirane-acrylic beads for obtaining phosphopeptides from casein.固定在环氧乙烷 - 丙烯酸珠上用于从酪蛋白中获取磷酸肽的胰蛋白酶的表征。
Z Ernahrungswiss. 1995 Jun;34(2):118-30. doi: 10.1007/BF01636945.