Bodanszky M, Martinez J, Priestley G P, Gardner J D, Mutt V
J Med Chem. 1978 Oct;21(10):1030-5. doi: 10.1021/jm00208a006.
The influence of tyrosine O-sulfate, the 27th residue in the sequence of cholecystokinin (pancreozymin) (CCK-PZ), on the contraction of gall bladder of guinea pigs and on the release of amylase in isolated pancreatic cells of the same animal was studied with an analogue of the biologically active C-terminal heptapeptide, CCK-PZ-(27--33). In the new analogue, tyrosine O-sulfate was replaced by epsilon-hydroxynorleucine O-sulfate. The synthetic peptide was found a full agonist in these tests, not quite as potent as the unaltered heptapeptide, but much more active than the previously prepared and studied serine O-sulfate containing analogue. Thus, the distance of the sulfate ester group from the peptide backbone has a major influence on the biological activity of CCK-PZ.
利用生物活性C末端七肽CCK-PZ-(27--33)的类似物，研究了胆囊收缩素（促胰酶素）（CCK-PZ）序列中第27位残基酪氨酸O-硫酸盐对豚鼠胆囊收缩以及对同一动物分离胰腺细胞中淀粉酶释放的影响。在新的类似物中，酪氨酸O-硫酸盐被ε-羟基正亮氨酸O-硫酸盐取代。在这些试验中发现该合成肽是一种完全激动剂，其效力不如未改变的七肽，但比先前制备和研究的含丝氨酸O-硫酸盐的类似物活性高得多。因此，硫酸酯基团与肽主链的距离对CCK-PZ的生物活性有重大影响。
