PROTEOLYTIC ACTIVITY IN BOVINE DENTAL PULP.
PROTEOLYTIC ACTIVITY IN BOVINE DENTAL PULP.
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牛牙髓中的蛋白水解活性。
DOI：
10.1016/0003-9861(65)90288-2
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发表时间：
1965
影响因子：
3.9
通讯作者：
G. Kalnitsky
中科院分区：
文献类型：
--
作者：
C. Schwabe;G. Kalnitsky
用吲哚三酮比色法研究了内源蛋白水解酶对牛牙髓的自溶作用。酸变性血红蛋白是牛牙髓组织蛋白酶的有效外源底物。最适的血红蛋白水解液是在pH值为4.0时。在严格控制的条件下(pH 5.0，56℃，60秒)，通过热分级将活性浓缩5倍。经Sephadex G-75过滤和羟基磷灰石柱层析得到进一步的活性浓度。在羟基磷灰石柱上，牛牙髓中存在的总的血红蛋白分解活性被分离成四个活性组份。其中两个组分的最适pH值有很大不同，分别为pH 3和pH 5。与原料相比，pH 3酶的相对纯度为80。
The autolysis of bovine dental pulp by endogenous proteolytic enzymes has been demonstrated by means of a colorimetric ninhydrin method. The activity is heat-labile and acts optimally at pH 3.0.Acid-denaturated hemoglobin proved to be a useful exogenous substrate for the cathepsins of bovine dental pulp. Optimal hemoglobin hydrolysis was shown to occur at pH 4.0. The activity was concentrated fivefold by heat fractionation under closely controlled conditions (pH 5.0, 56 ° C, 60 seconds). Further concentration of the activity was obtained by Sephadex G-75 filtration and hydroxyapatite column chromatography. The total hemoglobin-splitting activity present in bovine dental pulp was separated into four active fractions on the hydroxyapatite column. Two of the fractions differed considerably in their pH optima, which were observed to be at pH 3 and pH 5, respectively. The relative purification of the pH 3 enzyme was 80 when compared with the starting material.