Nagelschmidt M, Unger T
Wien Klin Wochenschr. 1977 Nov 11;89(21):735-8.
Synthetic PZ peptide, synthesized by Wünsch and Heidrich, was used as substrate to determine PZ peptidase activities in the sera of man, rabbit, guinea pig and mouse. The PZ peptidase from rabbit serum was purified 200 fold and characterized. The enzyme has an isoelectric point of 5.0 and pH optima at pH 7.2 and pH 7.9. Its behaviour on gel filtration points to a molecular weight of 60.000 dalton. The peptidase is inhibited by heavy metal ions, SH reagents and serum. Ca ions are EDTA are without any effect. In contrast to collagen peptidases from micro-organisms, the enzyme from rabbit serum does not attack native, but only denatured collagen. The results suggest that PZ peptidases participate in collagen breakdown by cleaving the collagen fragments which are released by the collagenases.
由温施和海德里希合成的合成PZ肽被用作底物,以测定人、兔、豚鼠和小鼠血清中的PZ肽酶活性。兔血清中的PZ肽酶被纯化了200倍并进行了特性鉴定。该酶的等电点为5.0,最适pH值为7.2和7.9。其在凝胶过滤中的行为表明分子量为60000道尔顿。该肽酶受到重金属离子、巯基试剂和血清的抑制。钙离子和乙二胺四乙酸没有任何影响。与微生物来源的胶原肽酶不同,兔血清中的酶不作用于天然胶原,而只作用于变性胶原。结果表明,PZ肽酶通过切割胶原酶释放的胶原片段参与胶原的分解。