Meuer S, Becker S, Hadding U, Bitter-Suermann D
Z Immunitatsforsch Immunobiol. 1978 Mar;154(2):135-46.
Highly purified guinea pig C3a was obtained after specific cleavage of isolated C3 by the alternative pathway enzyme VF-B in a one step procedure. It turned out to be a low molecular weight peptide with basic character (M.W. 9500; isoelectric point above 9.4). C3a represents an antigenetic determinant of its own in the native C3 molecule, different from the B determinant. Guinea pig C3a resistant to 100 degrees C for 10 minutes. Its smooth muscle contracting activity can be destroyed by trypsin and carboxypeptidase B. These findings indicate that guinea pig C3a is quite similar to human C3a.
通过替代途径酶VF - B对分离的C3进行一步特异性切割后,获得了高度纯化的豚鼠C3a。结果表明它是一种具有碱性特征的低分子量肽(分子量9500;等电点高于9.4)。C3a在天然C3分子中代表其自身的一个抗原决定簇,不同于B决定簇。豚鼠C3a在100摄氏度下耐受10分钟。其平滑肌收缩活性可被胰蛋白酶和羧肽酶B破坏。这些发现表明豚鼠C3a与人类C3a非常相似。