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- W2000135470 abstract "beta-Lactoglobulins from pooled milk (Sus scrofa domestica) are isolated and characterized. The complete primary structure of the major beta-lactoglobulin component I is presented. The amino-acid sequence was elucidated by automated Edman degradation of tryptic peptides and cyanogen bromide cleavage products in a liquid phase sequencer. The tryptic and cyanogen bromide peptides were separated by reverse-phase (RP-2) or size exclusion (TSK 2000 SW) high performance liquid chromatography. Pig beta-lactoglobulin is composed of only 159 amino acids in contrast to other beta-lactoglobulins which contain 162 or 166 amino acids. Sequence alignment with previously sequenced beta-lactoglobulins was obtained by introducing two gaps at positions 115 and 151-152. Thus bovine beta-lactoglobulin A reveals 62 amino-acid substitutions. The phylogenetic distance from horse beta-lactoglobulin I and II is indicated by 49.4% and 62% amino-acid exchanges, respectively. Pig beta-lactoglobulin is a mixture of two chains with Gln or Thr at position 119. The free thiol group is localized at position 59. The structural and functional aspects of beta-lactoglobulins and its role in vitamin A (retinol) transport are discussed." @default.
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- W2000135470 date "1986-01-01" @default.
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- W2000135470 title "Pig β-Lactoglobulin I<i>(Sus scrofa domestica,</i>Artiodactyla). The Primary Structure of the Major Component" @default.
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- W2000135470 doi "https://doi.org/10.1515/bchm3.1986.367.2.871" @default.
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