PROTEIN DENATURATION IN DOSAGE FORMS MEASURED BY DIFFERENTIAL SCANNING CALORIMETRY

被引：16

作者：

IZUTSU, K ^{[1
]}

YOSHIOKA, S ^{[1
]}

TAKEDA, Y ^{[1
]}

机构：

[1] NATL INST HYG SCI, 1-18-1 KAMIYOGA, SETAGAYA KU, TOKYO 158, JAPAN

来源：

CHEMICAL & PHARMACEUTICAL BULLETIN | 1990年 / 38卷 / 03期

关键词：

differential scanning calorimetry (DSC); protein dosage form; stability; thermal denaturation; β-galactosidase;

D O I：

10.1248/cpb.38.800

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The stability of β-galactosidase dosage forms was studied by differential scanning calorimetry (DSC). It was found that the observed enthalpy of thermal denaturation was approximately in proportion to remaining enzyme activity, and denaturation temperature was related to protein stability. These results suggest that DSC can be used to determine native proteins in dosage forms and to clarify the factors affecting protein stability. The DSC method seems to be more convenient than conventional activity assay methods, and useful to follow protein denaturation during the manufacturing process and storage of dosage forms. © 1990, The Pharmaceutical Society of Japan. All rights reserved.

引用

页码：800 / 803

页数：4

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