青霉菌的蛋白水解酶。一种胰蛋白酶原活化酶(肽酶a)的纯化和性质。

T. Hofmann , R. Shaw
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引用次数: 47

摘要

1.(1)从紫青霉(Penicillium janthinellum)生长培养基中分离到一种胰蛋白酶激活蛋白水解酶(肽酶A),纯化约60倍;在超离心机和电泳中均质。(2)该酶具有以下氨基酸组成:Lys5、His3、Asp36、Thr28、Ser42、Glu28、Pro12、Gly39、Ala23、Val22、Ileu12.5、Leu20、Tyr14、Phe19、Try4-5。3.(3)系统肽酶A-胰蛋白酶原遵循Michealis-Menten动力学,Km =(7.6±2)·10−6 M(0°,pH 3.4)。4.(4)肽酶A明显不作用于小肽,但容易降解载铁蛋白和牛血清白蛋白。牛血清白蛋白中约15%的肽键被水解。
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Proteolytic enzymes of Penicillium janthinellum

  • 1.

    (1) A trypsinogen-activating proteolytic enzyme (peptidase A) has been isolated from the growth medium of Penicillium janthinellum and purified about 60-fold; it is homogeneous in the ultra-centrifuge and on electrophoresis. Its molecular weight is 32 000.

  • 2.

    (2) The enzyme has the following amino acid composition: Lys5, His3, Asp36, Thr28, Ser42, Glu28, Pro12, Gly39, Ala23, Val22, Ileu12.5, Leu20, Tyr14, Phe19, Try4–5. It does not contain arginine, methione and half-crystine.

  • 3.

    (3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving Km = (7.6±2) · 10−6 M (at 0°, pH 3.4).

  • 4.

    (4) Peptidase A apparently does not act on small peptides, but readily degrades apoferritin and bovine serum albumin. About 15% of the peptide bonds in bovine serum albumin are hydrolysed.

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