Lazure C, Leduc R, Seidah N G, Chrétien M, Dubé J Y, Chapdelaine P, Frenette G, Paquin R, Tremblay R R
FEBS Lett. 1984 Sep 17;175(1):1-7. doi: 10.1016/0014-5793(84)80557-8.
Canine prostate fluids and seminal plasma contain a major androgen-dependent protein which was identified as a proteolytic enzyme exhibiting an Arg-esterase activity. This protease, as characterized, is shown to be present as a two-chain structure held together by at least one disulfide bridge and composed of approximately 220 amino acids. Amino acid sequence determination of both chains has revealed a clear homology to other known amino acid sequences of serine proteases. Furthermore, the comparison of the presented 58 amino acids of the Arg-esterase with the other sequences revealed a very strong homology (larger than 50%) to members of the kallikrein family. The two chain structure could thus result from autolysis of a single chain enzyme in the 'kallikrein autolysis loop'. Amino acid composition of the canine prostatic enzyme suggests that it is related, but not identical, to pancreatic canine kallikrein.
犬前列腺液和精浆中含有一种主要的雄激素依赖性蛋白,该蛋白被鉴定为一种具有精氨酸酯酶活性的蛋白水解酶。经鉴定,这种蛋白酶呈现为一种由至少一个二硫键连接在一起的双链结构,由大约220个氨基酸组成。两条链的氨基酸序列测定显示与其他已知丝氨酸蛋白酶的氨基酸序列有明显的同源性。此外,将精氨酸酯酶呈现的58个氨基酸与其他序列进行比较,发现与激肽释放酶家族成员有很强的同源性(大于50%)。因此,这种双链结构可能是由单链酶在“激肽释放酶自溶环”中自溶产生的。犬前列腺酶的氨基酸组成表明它与犬胰腺激肽释放酶有关,但并不相同。