@entity1707 beta-lactoglobulin I ( XXXX , Artiodactyla). The primary structure of the major component.

@entity1707 @entity1522 @entity1641 @entity12526 @entity535 @entity71930 @entity13518 @entity904 @entity71931 @entity7647 @entity1432 @entity2483 @entity291 @entity4001
beta-Lactoglobulins from pooled milk ( @entity12526 ) are isolated and characterized. The complete primary structure of the major @entity2483 is presented. The @entity535 sequence was elucidated by automated Edman degradation of tryptic peptides and @entity13518 cleavage products in a liquid phase sequencer. The tryptic and cyanogen @entity4001 peptides were separated by reverse-phase ( @entity71930 ) or size exclusion (TSK 2000 SW) high performance liquid chromatography. @entity1707 beta-lactoglobulin is composed of only 159 @entity1522 in contrast to other beta-lactoglobulins which contain 162 or 166 @entity1522 . Sequence alignment with previously sequenced beta-lactoglobulins was obtained by introducing two gaps at positions 115 and 151-152. Thus @entity291 beta-lactoglobulin A reveals 62 @entity535 substitutions. The phylogenetic distance from @entity1641 @entity71931 is indicated by 49.4% and 62% @entity535 exchanges, respectively. @entity1707 beta-lactoglobulin is a mixture of two chains with @entity7647 or Thr at position 119. The free @entity1432 group is localized at position 59. The structural and functional aspects of beta-lactoglobulins and its role in @entity904 ( @entity904 ) transport are discussed.
