Department of Biochemistry and Nutrition, The University of Nebraska, Lincoln, Nebraska 68503.
Plant Physiol. 1970 Sep;46(3):401-5. doi: 10.1104/pp.46.3.401.
The characteristics of a lipase preparation from the uredospores of Puccinia graminis (pers.) f. sp. tritici (Eriks. and Henn.) have been investigated. The majority of the lipolytic activity in disrupted uredospores was found to be associated with a lipid-containing, particulate fraction which sedimented at 5000g. With triolein as a substrate, both 1,3- and 1,2-diglycerides were formed. Ethylenediaminetetraacetate, p-chloromercuribenzoic acid, and Hg(2+) strongly inhibited the activity. A pH optimum of 6.7 was observed. The sensitivity of the preparation to higher temperatures was indicated by a complete loss of activity when the preparation was preincubated at 25 C or above for 30 minutes. A temperature optimum of 15 C for the enzyme is strikingly similar to the temperature optimum for germination of the uredospores. The possible relationship between the sensitivity of the enzyme and the germination process is discussed.
已研究来自禾柄锈菌（Eriks. 和 Henn.）的冬孢子的脂肪酶制剂的特性。在破碎的冬孢子中，大多数脂肪分解活性与含有脂质的颗粒部分相关，该部分在 5000g 时沉降。以三油酸甘油酯为底物，形成 1,3-和 1,2-二甘油酯。乙二胺四乙酸、对氯汞苯甲酸和 Hg(2+)强烈抑制活性。观察到 pH 值为 6.7 时的最佳 pH 值。制剂对较高温度的敏感性表明，当制剂在 25°C 或更高温度下预孵育 30 分钟时，活性完全丧失。酶的最适温度为 15°C，与冬孢子萌发的最适温度非常相似。讨论了酶的敏感性与萌发过程之间的可能关系。
