Aguilar M B, Soyez D, Falchetto R, Arnott D, Shabanowitz J, Hunt D F, Huberman A
Department of Biochemistry, Instituto Nacional de la Nutrición S. Zubirán, Tlalpan, Mexico City, Mexico.
Peptides. 1995;16(8):1375-83. doi: 10.1016/0196-9781(95)02024-1.
The primary structure of the neurohormone crustacean hyperglycemic hormone (CHH-II) was determined by means of enzymatic digestions, manual Edman degradation, and mass spectrometry. CHH-II is a 72 residue peptide (molecular mass 8388 Da), with six cysteines forming three disulfide bridges that connect residues 7-43, 23-39, and 26-52. The peptide has blocked N- and C-termini, and lacks tryptophan, histidine, and methionine. The CHH-I and CHH-II of Procambarus bouvieri have identical sequences and elicit levels of hyperglycemia that are not distinguishable. The difference between the two isomorphs consists in a posttranslational modification of a L-Phe in CHH-I to a D-Phe in CHH-II at the third position from the N-terminus.
通过酶解、手动埃德曼降解和质谱分析确定了神经激素甲壳类高血糖激素（CHH-II）的一级结构。CHH-II是一种由72个氨基酸残基组成的肽（分子量8388道尔顿），有六个半胱氨酸形成三个二硫键，连接第7-43、23-39和26-52位的残基。该肽的N端和C端被封闭，并且缺乏色氨酸、组氨酸和甲硫氨酸。布氏原螯虾的CHH-I和CHH-II具有相同的序列，引发的高血糖水平无法区分。这两种同形体之间的差异在于，CHH-I中N端第三位的L-苯丙氨酸在翻译后修饰为CHH-II中的D-苯丙氨酸。
