Richter W O, Naudé R J, Oelofsen W, Schwandt P
Endocrinology. 1987 Apr;120(4):1472-6. doi: 10.1210/endo-120-4-1472.
beta-Endorphin stimulates glycerol release from adipose tissue in vitro in the rabbit. Thirty different amino acid sequences of this peptide were tested for lipolytic activity. Four turned out to be active: porcine and human beta-endorphin-(1-31), human beta-endorphin-(6-31), and human beta-endorphin-(1-5)-(16-31). Structure-activity investigations showed that for the lipolytic action of beta-endorphin the C-terminal part [longer than beta-endorphin-(27-31)] is relatively important. Of special importance seems to be the C-terminal amino acid residue, because none of the sequences lacking the last two amino acid residues was lipolytically active. Furthermore, a different lipolytic response to beta-endorphin was obtained in starved, ad libitum-fed, and starved-refed animals, showing that the regulation of the lipolytic potency is not only mediated by peptide concentrations in the medium.
β-内啡肽在体外可刺激兔脂肪组织释放甘油。对该肽的30种不同氨基酸序列进行了脂解活性测试。结果发现其中4种具有活性：猪和人β-内啡肽-（1-31）、人β-内啡肽-（6-31）以及人β-内啡肽-（1-5）-（16-31）。构效关系研究表明，对于β-内啡肽的脂解作用而言，C末端部分[长于β-内啡肽-（27-31）]相对重要。C末端氨基酸残基似乎尤为重要，因为缺少最后两个氨基酸残基的序列均无脂解活性。此外，在饥饿、随意进食以及饥饿-再喂食的动物中，对β-内啡肽的脂解反应有所不同，这表明脂解效力的调节不仅由培养基中的肽浓度介导。
