烟曲霉酸性蛋白酶的物理化学性质
Physico-chemical properties of the acid proteinase from A. fumigatus.
作者信息
Panneerselvam M, Dhar S C
出版信息
Ital J Biochem. 1981 Jan-Feb;30(1):63-74.
The physico-chemical properties of the purified acid proteinase were investigated. This enzyme was found to hydrolyze hemoglobin maximally among the different substrates used. The maximum hydrolysis of hemoglobin was found at pH 2.8 and 45 degrees C in 30 min. Km value of 5.5 X 10(-4) M was obtained from the Lineweaver Burk plot for the hydrolysis of hemoglobin. The enzyme was found to be most stable at pH 4.9. The maximum stability of the enzyme was observed with 2 per cent casein as a stabilising agent. It was found to have a molecular weight 37,500 consisting of 298 aminoacid residues. The partial specific volume of the acid proteinase was found to be 0.734 ml/g. Leucine and alanine were the amino and carboxy terminal aminoacids of the acid proteinase respectively.
对纯化的酸性蛋白酶的物理化学性质进行了研究。发现该酶在所用的不同底物中对血红蛋白的水解作用最大。在pH 2.8和45℃下30分钟时发现血红蛋白的最大水解。通过Lineweaver Burk图得到血红蛋白水解的Km值为5.5×10(-4)M。发现该酶在pH 4.9时最稳定。以2%的酪蛋白作为稳定剂时观察到该酶的最大稳定性。发现其分子量为37500，由298个氨基酸残基组成。酸性蛋白酶的比容为0.734 ml/g。亮氨酸和丙氨酸分别是酸性蛋白酶的氨基末端和羧基末端氨基酸。
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