COMPARTMENTATION OF TRYPTOPHAN-SYNTHASE-PROTEOLYZING SYSTEM IN SACCHAROMYCES-CEREVISIAE
COMPARTMENTATION OF TRYPTOPHAN-SYNTHASE-PROTEOLYZING SYSTEM IN SACCHAROMYCES-CEREVISIAE
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DOI：
10.1111/j.1432-1033.1974.tb03748.x
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发表时间：
1974-01-01
期刊：
影响因子：
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通讯作者：
HOLZER, H
中科院分区：
文献类型：
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作者：
HASILIK, A;MULLER, H;HOLZER, H
利用酵母球质体代谢裂解物的Ficoll梯度分离制备液泡、线粒体和细胞质组分。色氨酸合成酶活性仅存在于可溶性部分。蛋白酶A、B和C以及色氨酸合酶灭活活性主要存在于液泡部分。可溶性部分存在抑制pröteinase和色氨酸合酶灭活酶的热稳定活性。色氨酸合酶和色氨酸合酶灭活活性的亚细胞分离解释了为什么在静止酵母细胞的粗提取物中，色氨酸合酶活性很高，尽管色氨酸合酶灭活活性很高。新鲜制备的酵母球质体液泡部分的蛋白酶不能使外部添加的色氨酸合成酶失活，除非细胞器被超声或渗透冲击破坏。
Ficoll‐gradient fractionation of a metabolic lysate from yeast spheroplasts was used to prepare vacuole, mitochondria and cytosol fractions. Tryptophan synthase activity was exclusively found in the soluble fraction. Proteinases A, B and C as well as the tryptophan‐synthase‐inactivating activity were mainly found in the vacuole fraction. The heat‐stable activities inhibiting pröteinase and tryptophan‐synthase‐inactivating enzyme appeared in the soluble fraction. The subcellular separation of tryptophan synthase and the tryptophan‐synthase‐inactivating activities explains why in crude extracts from stationary yeast cells, high tryptophan synthase activities are observed in spite of high tryptophan‐synthase‐inactivating activity. The proteinases of a freshly prepared vacuole fraction from yeast spheroplasts are unable to inactivate externally added tryptophan synthase unless the organelles are disrupted by sonication or osmotic shock.