Puliti M, Cambi S, Buffoni F
Department of Preclinical and Clinical Pharmacology, University of Florence, Firenze, Italy.
Comp Biochem Physiol B Biochem Mol Biol. 1996 Oct;115(2):159-65. doi: 10.1016/0305-0491(96)00046-6.
Lung, heart tissues and blood plasma of guinea pigs were investigated to see if tissue-bound semicarbazide-sensitive amine oxidase activities with a high affinity for benzylamine (Bz.SSAO) were present in this species as well as in others. This paper shows that these enzymic activities are present in guinea pig lung and heart where they are mainly localized in the cytosol and in microsomal fraction. These activities have a high affinity for benzylamine and appear unable to oxidize histamine at an appreciable rate in agreement with the observation that the purified Bz.SSAO of guinea pig skin shows weak histaminase activity. These guinea pig Bz.SSAO activities show some homology with the pure pig plasma benzylamine oxidase. They crossreact with the antibodies raised in the rabbit against the pig plasma enzyme. Benzylamine oxidase activity was also found in guinea pig blood plasma.
对豚鼠的肺、心脏组织和血浆进行了研究,以确定该物种以及其他物种中是否存在对苄胺具有高亲和力的组织结合型氨基脲敏感胺氧化酶活性(Bz.SSAO)。本文表明,这些酶活性存在于豚鼠的肺和心脏中,主要定位于胞质溶胶和微粒体部分。这些活性对苄胺具有高亲和力,并且似乎无法以可观的速率氧化组胺,这与豚鼠皮肤纯化的Bz.SSAO显示出较弱的组胺酶活性的观察结果一致。这些豚鼠Bz.SSAO活性与纯猪血浆苄胺氧化酶具有一些同源性。它们与兔体内针对猪血浆酶产生的抗体发生交叉反应。在豚鼠血浆中也发现了苄胺氧化酶活性。