McDonald T J, Jörnvall H, Tatemoto K, Mutt V
FEBS Lett. 1983 Jun 13;156(2):349-56. doi: 10.1016/0014-5793(83)80527-4.
Porcine intestinal gastrin-releasing peptide (GRP) has been demonstrated to be structurally identical to the previously characterized gastric GRP. Ion-exchange and high-performance liquid chromatography of porcine intestinal extracts have identified two variant GRP forms. Studies on one of these variant forms suggest that a beta-aspartyl shift has occurred in the Asn-His structure of GRP; such a modification in an Asn-His structure occurring in a natural peptide or protein has not been previously reported. This variant GRP, although retaining bioactivity, appears to have reduced potency in elevating canine plasma gastrin levels.
猪肠道胃泌素释放肽（GRP）已被证明在结构上与先前鉴定的胃GRP相同。对猪肠道提取物进行离子交换和高效液相色谱分析，已鉴定出两种GRP变体形式。对其中一种变体形式的研究表明，GRP的天冬酰胺-组氨酸结构中发生了β-天冬氨酰移位；天然肽或蛋白质中天冬酰胺-组氨酸结构的这种修饰此前尚未见报道。这种变体GRP虽然保留了生物活性，但在提高犬血浆胃泌素水平方面的效力似乎有所降低。
