Halliday J A, Bell K, Shaw D C
Department of Physiology and Pharmacology, University of Queensland, Brisbane, Australia.
Biochim Biophys Acta. 1991 Mar 8;1077(1):25-30. doi: 10.1016/0167-4838(91)90521-z.
The amino acid sequence of feline beta-lactoglobulin (designated II) has been determined. The protein chain is 163 amino acids long with a relative molecular mass of 18,558. The primary structure was determined by sequencing of native protein (residues 1-25), BPNS-skatole cleavage fragments and the peptides obtained by proteolytic cleavage with V8 proteinase and TPCK-trypsin. Feline beta-lactoglobulin II has 53 and 57% positional identities with bovine beta-lactoglobulin A and equine beta-lactoglobulin I, respectively, and approx. 68% with a revised sequence of equine beta-lactoglobulin II. The equine beta-lactoglobulin II sequence was re-examined between positions 78 and 122 resulting in a major revision in this area with only a single insertion to give a total of 163 residues.
猫β-乳球蛋白（命名为II）的氨基酸序列已被确定。蛋白质链由163个氨基酸组成，相对分子质量为18558。其一级结构是通过对天然蛋白质（第1-25位残基）、BPNS-粪臭素裂解片段以及用V8蛋白酶和TPCK-胰蛋白酶进行蛋白水解裂解得到的肽段进行测序来确定的。猫β-乳球蛋白II与牛β-乳球蛋白A和马β-乳球蛋白I的位置同一性分别为53%和57%，与马β-乳球蛋白II的修订序列约为68%。对马β-乳球蛋白II序列在第78至122位之间进行了重新检查，导致该区域有重大修订，仅插入了一个残基，使总残基数达到163个。
