摘要:
An extracellular leucine aminopeptidase was isolated from the culture medium of Streptomyces therrnonitrificans which is a Zn.sup.2+ -dependent metalloenzyme which comprises an amino acid sequence Lys-Phe-Ser-Lys-Lys-Phe-Asn-Glu (SEQ ID NO: 3) at the N-terminal thereof, and amino acid sequences of Glu-Pro-Gly-Thr-Gly-Ala-Leu-Glu-Pro (SEQ ID NO: 4) and Asn-Pro-Asp-Ile-Val-Tyr (SEQ ID NO: 5) at other regions thereof. The aminopeptidase has a pH optimum of 7.5 to 9.0, a temperature optimum of 30.degree. to 50.degree. C., and an apparent molecular weight as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions of 41 to 45 kDa, and as determined by gel filtration under native state conditions of 36 to 40 kDa.
摘要翻译:从作为Zn 2+依赖性金属酶的链霉菌(Streptomyces thernnitrificans)的培养基中分离出细胞外亮氨酸氨基肽酶,其包含氨基酸序列Lys-Phe-Ser-Lys-Lys-Phe-Asn-Glu(SEQ ID NO:3) Glu-Pro-Gly-Thr-Gly-Ala-Leu-Glu-Pro(SEQ ID NO:4)和Asn-Pro-Asp-Ile-Val-Tyr的氨基酸序列(SEQ ID NO: :5)其他地区。 氨基肽酶的pH最佳值为7.5〜9.0,最适温度为30〜50℃,表观分子量由十一烷基硫酸钠聚丙烯酰胺凝胶电泳法测定,在41〜45kDa的还原条件下测定, 在36至40kDa的天然状态下进行凝胶过滤。