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弹性蛋白酶(Elastase 即胰肽酶)的活性可用天然底物(弹性蛋白,elastin)或合成的底物测定。本文报道,采用醋酸1-丙氨酰-1-丙氨酰-1-丙氨酰甲酯(Ala_30Me)作为底物同时测定弹性酶中酯酶和肽酶二种活性的测定方法。利用酯酶的活性可使Ala_3OMe分离成Ala_3和MeOH,根据消耗的Ala_3OMe以及反应形成的Ala_3检测酯酶的活性。肽酶的活性可同样以Ala_3OMe为底物反应,生成Ala_2和Ala-OMe,根据形成的Ala_2检测肽酶活性。而其它朊酶如骨胶原酶与Ala_3OMe作用,则反应先产生Ala_3,然后继续分离Ala_2和Ala。本文报道的方法可区别出弹性酶及其它酶中的酯酶或肽酶。
Elastase (ie, trypsin) activity can be measured using natural substrates (elastin) or synthetic substrates. This paper reports the simultaneous determination of the activity of esterase and peptidase in elastase using 1-alanyl-1-alanyl-1-alanyl acetate (Ala_30Me) as a substrate. Ala_3OMe can be separated into Ala_3 and MeOH using the activity of esterase, and the activity of esterase can be detected based on Ala_3OMe consumed and Ala_3 formed by the reaction. Peptidase activity can also Ala3OMe as a substrate reaction to generate Ala2 and Ala-OMe, based on the formation of Ala2 peptidase activity test. While other proteases such as collagenase and Ala_3OMe, the reaction produces Ala_3, and then continue to separate Ala_2 and Ala. The methods reported here distinguish esterase or peptidase in elastase and other enzymes.