Goldberg G I, Wilhelm S M, Kronberger A, Bauer E A, Grant G A, Eisen A Z
J Biol Chem. 1986 May 15;261(14):6600-5.
We have determined the complete sequence of the cDNA clone representing the full size human skin collagenase mRNA. Collagenase is synthesized in preproenzyme form, Mr 54,092, with a 19 amino acid long signal peptide. The primary secretion products of the enzyme consist of a minor glycosylated form, Mr 57,000, and a major unmodified polypeptide of predicted Mr 51,929. Proteolytic activation of human skin procollagenase results in removal of 81 amino acid residues from the amino-terminal portion of the proenzyme. Both potential N-glycosylation sites are contained within the proteolytically activated form of the enzyme. The primary structure of the coding region of the presented clone is homologous to an oncogene-induced rat protein whose function is still unknown, although preliminary observations suggest that it is not rat skin collagenase.
我们已经确定了代表全长人皮肤胶原酶mRNA的cDNA克隆的完整序列。胶原酶以前酶原形式合成，分子量为54,092，带有一个19个氨基酸长的信号肽。该酶的主要分泌产物包括一种较小的糖基化形式，分子量为57,000，以及一种预测分子量为51,929的主要未修饰多肽。人皮肤前胶原酶的蛋白水解激活导致从前酶原的氨基末端部分去除81个氨基酸残基。两个潜在的N-糖基化位点都包含在该酶的蛋白水解激活形式中。所呈现克隆的编码区的一级结构与一种癌基因诱导的大鼠蛋白同源，其功能仍然未知，尽管初步观察表明它不是大鼠皮肤胶原酶。
