Oike Y, Kimata K, Shinomura T, Suzuki S
Biochem J. 1980 Oct 1;191(1):203-7. doi: 10.1042/bj1910203.
Significant amounts of proteinase activity have been found in chondroitin ABC lyase (EC 4.2.2.4), chondroitin AC II lyase and endo-beta-D-galactosidase (keratanase) from commercial sources. It would appear, therefore, that certain earlier biochemical and histochemical studies, which employed these commercial enzyme preparations for their presumed ability to degrade only glycosaminoglycans, may require re-evaluation. A mixture of EDTA, N-ethylmaleimide, phenylmethanesulphonyl fluoride and pepstatin abolishes the effect of the contaminating proteinases on proteoglycan with less significant effect on the chondroitin lyase or keratanase activity.
已发现来自商业来源的软骨素ABC裂解酶(EC 4.2.2.4)、软骨素AC II裂解酶和内切-β-D-半乳糖苷酶(角质酶)中存在大量蛋白酶活性。因此,某些早期的生物化学和组织化学研究,使用这些商业酶制剂是因为假定它们仅具有降解糖胺聚糖的能力,现在可能需要重新评估。乙二胺四乙酸(EDTA)、N-乙基马来酰亚胺、苯甲基磺酰氟和胃蛋白酶抑制剂的混合物可消除污染蛋白酶对蛋白聚糖的影响,而对软骨素裂解酶或角质酶活性的影响较小。