Proteolytic enzymes of Penicillium janthinellum

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects Pub Date : 1964-12-23 DOI:10.1016/0926-6569(64)90014-8

T. Hofmann , R. Shaw

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引用次数: 47

Abstract

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, Ileu_12.5, Leu₂₀, Tyr₁₄, Phe₁₉, Try_4–5. It does not contain arginine, methione and half-crystine.
3.
(3) The system peptidase A-trypsinogen follows Michealis-Menten kinetics, giving K_m = (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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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。

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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Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects

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