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S-PI对香菇酸性蛋白酶的抑制机理及其促进出菇的生化解释 被引量:5

MECHANISM OF S-PI INHIBITION TO THE ACTIVITY OF ACID PROTEASE AND EXPLANATION OF ITS PROMOTIN TO FRUITING OF LENT IN US EDODES
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摘要 S-PI对纯化的香菇酸性蛋白酶具有强烈的抑制作用,10μmol/L的S-PI可使酶活降低77%,这种抑制属于可逆竞争抛物线型抑制。经25μmol/L酸性蛋白酶水解6小时后,香菇胞外酸性磷酸酶的活性从24.6单位降低到20.8单位,同时C_1酶和c_x酶的活性分别比对照降低了76%和58%,这表明香菇酸性蛋白酶不仅直接左右着香菇发育的氮代谢,同时也间接地影响着碳代谢及能量转换。 S-PI shows a strong inhibition to purified acid protease from Len-tinus edodes. 10μmol/L can lead the decrease of the acid protease activity to 23%, this belongs to reversible, parabolic, competitive inhibition. After 6 hour hydrolysis with 25μmol/L acid protease, the activity of acid phosphatase decreased from 24.6 units to 20.8 units, at the same time 76% and 58% activities of two cellulase are lost. This indicates that the acid protease affects the development of Lentinus edodes not only directly on the metabolism of nitrogen but also indirectly on the metabolism of carbon and energy.
出处 《真菌学报》 CSCD 北大核心 1994年第3期223-228,共6页
基金 上海市科委青年基金
关键词 香菇 S-PI 酸性蛋白酶 食用菌 Lentinus edodes, S-PI, Acid protease, Acid phosphatase, Cellulase
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  • 1Eiji Ichishima,Hiroyuki Kumagai,Katsumi Tomoda. Substrate specificity of carboxyl proteinase fromPycnoporus coccineus, a wood-deteriorating fungus[J] 1980,Current Microbiology(6):333~337 被引量:1
  • 2Gertrud Wendelberger-Schieweg,Aloys Hüttermann. Amino acid pool and protein turnover during differentiation (spherulation) ofPhysarum polycephalum[J] 1978,Archives of Microbiology(1):27~34 被引量:1

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