Lynn K R, Brockbank W J, Clevette N A
Biochim Biophys Acta. 1980 Mar 14;612(1):119-25. doi: 10.1016/0005-2744(80)90284-3.
Two groups of asclepains (EC 3.4.22.7) isolated from the latex of Asclepias syriaca L. (milkweed) were each separated into five homogeneous enzymes. The members of each group are of similar amino acid composition, and leucine is the common N-terminal residue. Michaelis values are reported for each of the component cysteinyl proteases of milkweek latex, and are compared with those of analogous enzymes from other plant sources. The asclepains all catalysed the hydrolysis of insulin B chain to yield similar two-dimensional maps. The peptides produced from one such digestion were characterized and scission points were defined and compared with those for papain.
从叙利亚马利筋（乳草）的乳汁中分离出的两组天冬蛋白酶（EC 3.4.22.7）各自被分离成五种均一的酶。每组的成员具有相似的氨基酸组成，且亮氨酸是常见的N端残基。报道了乳草乳汁中各组成半胱氨酸蛋白酶的米氏值，并与来自其他植物来源的类似酶进行了比较。所有天冬蛋白酶都催化胰岛素B链的水解，以产生相似的二维图谱。对一次这样的消化产生的肽进行了表征，确定了裂解点，并与木瓜蛋白酶的裂解点进行了比较。
