Chr Lorenzen P, Schieber A, Brückner H, Schlimme E
Institut für Chemie und Physik der Bundesanstalt für Milchforschung, Kiel, Deutschland.
Nahrung. 1996 Feb;40(1):7-11. doi: 10.1002/food.19960400103.
Characterization of pancreatic casein plasteins. In the course of the plastein reaction hydrophobic peptides concentrate mainly in the aggregates (plasteins), whilst hydrophilic peptides remain in solution (supernatant). Liquid chromatographic and sequence analytical studies of pancreatic casein plasteins have shown that the aggregates consist mainly of the free amino acids tyrosine, phenylalanine and tryptophan. Plasteins contain, in addition, short-chain peptides, particularly from the C-terminal of beta-casein. Characterization of the functional properties of the plasteins has shown clearly that aggregation of the short-chain peptides and free amino acids is brought by non-covalent, hydrophobic and ionogenic interactions. In the supernatants resulting from the plastein reaction caseinophosphopeptide sequences, in particular from alpha s-casein, were determined.
胰酪蛋白塑解蛋白的特性。在塑解蛋白反应过程中，疏水性肽主要集中在聚集体（塑解蛋白）中，而亲水性肽则保留在溶液（上清液）中。对胰酪蛋白塑解蛋白的液相色谱和序列分析研究表明，聚集体主要由游离氨基酸酪氨酸、苯丙氨酸和色氨酸组成。此外，塑解蛋白还含有短链肽，特别是来自β-酪蛋白C末端的短链肽。对塑解蛋白功能特性的表征清楚地表明，短链肽和游离氨基酸的聚集是由非共价、疏水和离子相互作用引起的。在塑解蛋白反应产生的上清液中，测定了酪蛋白磷酸肽序列，特别是来自αs-酪蛋白的序列。
