Schwalb M N
J Biol Chem. 1977 Dec 10;252(23):8435-9.
The basidiomycete Schizophyllum commune produces three chromatographically distinguishable proteases which are capable of attack on a variety of other enzymes from S. commune and other sources. These proteases, which are produced during a specific phase of the development cycle, exhibit typical enzyme kinetic patterns, are active in the neutral to weakly alkaline pH range and are inhibited by phenylmethylsulfonyl fluoride, soybean trypsin inhibitor, and ovomucoid. No pattern of specificity toward the test enzymes could be discerned. The proteases co-purify with the activity which causes the increase in cold lability of S. commune phosphoglucomutase reported previously. In addition, one of the protease enzymes could be purified to the point where it had no significant ability to release trichloroacetic acid products from denatured substrates at pH 3 or pH 7. When undenatured hemoglobin was used as a substrate, the purified protease releases a relatively large molecular weight nonheme peptide. Relatively large peptides are also formed after proteolysis of rabbit muscle phosphoglucomutase. These results suggest that the protease carries out only limited proteolysis.
担子菌裂褶菌可产生三种能用色谱法区分的蛋白酶，它们能够作用于来自裂褶菌和其他来源的多种其他酶。这些蛋白酶在发育周期的特定阶段产生，呈现出典型的酶动力学模式，在中性至弱碱性pH范围内具有活性，并被苯甲基磺酰氟、大豆胰蛋白酶抑制剂和卵类粘蛋白抑制。未发现对测试酶的特异性模式。这些蛋白酶与先前报道的导致裂褶菌磷酸葡萄糖变位酶冷不稳定性增加的活性共同纯化。此外，其中一种蛋白酶可纯化到在pH 3或pH 7时从变性底物释放三氯乙酸产物的能力不显著的程度。当未变性的血红蛋白用作底物时，纯化的蛋白酶会释放出相对大分子量的非血红素肽。兔肌肉磷酸葡萄糖变位酶经蛋白水解后也会形成相对大的肽。这些结果表明该蛋白酶仅进行有限的蛋白水解。
