PURIFICATION AND CHARACTERIZATION OF A PROPHENOLOXIDASE ACTIVATING ENZYME FROM CRAYFISH BLOOD-CELLS

被引：74

作者：

ASPAN, A

STURTEVANT, J

SMITH, VJ

SODERHALL, K

机构：

[1] UNIV UPPSALA, DEPT PHYSIOL BOT, BOX 540, S-75121 UPPSALA, SWEDEN

[2] UNIV ST ANDREWS, GATTY MARINE LAB, DEPT BIOL & PRECLIN MED, ST ANDREWS KY16 8LB, SCOTLAND

来源：

INSECT BIOCHEMISTRY | 1990年 / 20卷 / 07期

关键词：

SERINE PROTEINASE; PROPHENOLOXIDASE ACTIVATING ENZYME; CRAYFISH PROTEINASE;

D O I：

10.1016/0020-1790(90)90085-9

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 proteinase was purified from crayfish haemocytes by affinity chromatography on heparin-sepharose and phenyl-sepharose, followed by DEAE-cellulose ion-exchange chromatography. This proteinase could mediate the conversion of prophenoloxidase (proPO) to its active form, phenoloxidase (PO), and its was therefore designated a prophenoloxidase activating enzyme, ppA. The purified ppA had a molecular mass of about 36,000 Da. Since ppA was a proteinase able to cleave chromogenic peptide substrates of trypsin, and serine proteinase inhibitors were strongly inhibitory towards ppA v activity, the enzyme appeared to be a serine type proteinase. It exhibited maximal enzyme activity at neutral and slightly alkaline pH, and was sensitive to heat inactivation at 58-degrees-C.

引用

页码：709 / +

页数：1

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