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正常及异常(PSE)肌肉中糖原磷酸化酶b的纯化及同工酶组成

Purification and isoenzymic composition of glycogen phosphorylase b from normal and abnormal (PSE) muscles.

作者信息

Lopez Buesa P, Schwägele F, Honikel K O

机构信息

Institut für Chemie und Physik, Bundesanstalt für Fleischforschung, Kulmbach, Germany.

出版信息

Z Lebensm Unters Forsch. 1995 Jul;201(1):30-4. doi: 10.1007/BF01193197.

DOI:10.1007/BF01193197
PMID:7571864
Abstract

Ion exchange chromatography and preparative isoelectric focusing allowed the identification of five isoenzymes of glycogen phosphorylase b from the longissimus dorsi muscle of normal pigs and those prone to having pale, soft and exudative (PSE) muscle. The isoelectric point of the isoenzymes varied in the pH range from 6.29 to 6.55. One of them, with an isoelectric point at about a pH of 6.49, accounts for 65% of the total glycogen phosphorylase b activity. No significant differences between normal and PSE-prone pigs were observed in the total glycogen phosphorylase b activity and in the isoenzyme distribution pattern. It is concluded that the fast glycogen turnover in PSE-prone pigs is not due to a different isoenzyme pattern of phosphorylase b.

摘要

离子交换色谱法和制备性等电聚焦法可用于鉴定正常猪和易产生苍白、柔软和渗出性(PSE)肌肉的猪背最长肌中糖原磷酸化酶b的五种同工酶。这些同工酶的等电点在pH 6.29至6.55范围内变化。其中一种等电点约为pH 6.49的同工酶,占糖原磷酸化酶b总活性的65%。在糖原磷酸化酶b的总活性和同工酶分布模式方面,未观察到正常猪和易患PSE猪之间存在显著差异。得出的结论是,易患PSE猪的糖原快速周转并非由于磷酸化酶b的同工酶模式不同。

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