Isolation and rapid sequence characterization of two novel bovine beta-lactoglobulins I and J.
Two novel bovine beta-lactoglobulins I and J have been isolated from bovine milk and characterized by isoelectric focusing. Their primary structure was determined by a very rapid method consisting of a combination of Edman sequencing, mass analysis, and ladder sequencing by mass spectrometry. We found that both new beta-lactoglobulins are of the bovine beta-lactoglobulin B-variant type. beta-lactoglobulin I shows Gly instead of Glu at position 108, whereas beta-lactoglobulin J shows a Pro-to-Leu exchange at position 126.
Godovac-Zimmermann
J
J
Institut für Molekulare Biotechnologie, Jena, Germany.
Krause
I
I
Baranyi
M
M
Fischer-Frühholz
S
S
Juszczak
J
J
Erhardt
G
G
Buchberger
J
J
Klostermeyer
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007782:Lactoglobulins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013058:Mass Spectrometry; D008892:Milk / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009943:Organophosphorus Compounds / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D017421:Sequence Analysis; D017385:Sequence Homology; D014357:Trypsin / Q000378:metabolism
C043517:2-(4-isothiocyanatophenoxy)-1,3,2-dioxaphosphinene 2-oxide; D007782:Lactoglobulins; D009943:Organophosphorus Compounds; D010455:Peptides; D014357:Trypsin