Rao A J, Ramachandran J, Li C H
Proc Soc Exp Biol Med. 1976 Feb;151(2):285-7. doi: 10.3181/00379727-151-39193.
The rat hepatic ornithine decarboxylase stimulating activity of plasmin-modified human growth hormone and its two peptide fragments has been investigated. The activity was completely retained after plasmin treatment. The NH2-terminal fragment [Cys (Cam)53-HGH-(1-134)] retained 10% of the activity, whereas the COOH-terminal fragment [Cys (Cam) 165, 182, 189-(141-191)] was not active. The lipolytic activity of human growth hormone was greatly reduced after plasmin treatment, as examined in isolated rabbit adipocytes. It is suggested that the structural requirements for the lipolytic activity of the hormone are different from those required for stimulation of ornithine decarboxylase activity.
已对纤溶酶修饰的人生长激素及其两个肽片段的大鼠肝脏鸟氨酸脱羧酶刺激活性进行了研究。纤溶酶处理后，该活性完全保留。氨基末端片段[Cys (Cam)53-HGH-(1-134)]保留了10%的活性，而羧基末端片段[Cys (Cam) 165, 182, 189-(141-191)]没有活性。如在分离的兔脂肪细胞中所检测的，纤溶酶处理后人生长激素的脂解活性大大降低。提示该激素脂解活性的结构要求与刺激鸟氨酸脱羧酶活性所需的结构要求不同。
