PURIFICATION OF THE 200 KDA HEMOCYTE MEMBRANE-PROTEIN OF SARCOPHAGA-PEREGRINA AND ITS SPECIFIC INTERACTION WITH FAT-BODY

被引：16

作者：

KOBAYASHI, H ^{[1
]}

KURATA, S ^{[1
]}

NATORI, S ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN

来源：

INSECT BIOCHEMISTRY | 1991年 / 21卷 / 05期

关键词：

D O I：

10.1016/0020-1790(91)90105-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A 200 kDa protein specifically expressed on the surface of pupal hemocytes of Sarcophaga peregrina was purified from the hemocyte membrane. This protein has been suggested to participate in dissociation of the fat body in the pupal stage of this insect. This protein was found to inhibit the dissociation of the fat body in vitro. Furthermore, it was shown to bind to the fat body and the binding could be saturated. These results suggested that pupal hemocytes expressing the 200 kDa protein interact directly with specific binding sites on the basement membrane of the fat body when they disintegrate this tissue.

引用

页码：517 / 522

页数：6

共 13 条

[1]

Bodenstein D., 1950, BIOL DROSOPHILA, P275

[2]

Dean R.L., 1985, P155

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