Skytt A, Strömqvist M, Egelrud T
Astra-Hässle AB, Umeå, Sweden.
Biochem Biophys Res Commun. 1995 Jun 15;211(2):586-9. doi: 10.1006/bbrc.1995.1853.
Stratum corneum chymotryptic enzyme (SCCE) is a new human serine proteinase expressed by keratinocytes in the epidermis. Its function may be to catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous sheeding of cells from the skin surface. In this work the primary substrate specificity of recombinant SCCE was determined with oxidized bovine insulin B chain as substrate. Cleavage products were separated with high performance liquid chromatography and analyzed by amino acid sequence analysis and mass spectrometry. Cleavage sites were localized to Leu 6-cysteic acid 7, Tyr 16-Leu 17, Phe 25-Tyr 26, and Tyr 26-Thr 27 in insulin B chain. It is concluded that SCCE belongs to the family of serine endoproteinases specific for amino acid residues with aromatic side chains in the P1 position.
角质层胰凝乳蛋白酶（SCCE）是一种由表皮角质形成细胞表达的新型人类丝氨酸蛋白酶。其功能可能是在皮肤表面细胞持续脱落过程中，催化皮肤角质层细胞间黏附结构的降解。在这项研究中，以氧化牛胰岛素B链为底物测定了重组SCCE的主要底物特异性。用高效液相色谱法分离裂解产物，并通过氨基酸序列分析和质谱法进行分析。胰岛素B链中的裂解位点定位于Leu 6-半胱磺酸7、Tyr 16-Leu 17、Phe 25-Tyr 26和Tyr 26-Thr 27。得出的结论是，SCCE属于对P1位置具有芳香族侧链的氨基酸残基具有特异性的丝氨酸内切蛋白酶家族。
