TY - JOUR
T1 - Characterization of baboon (Papio hamadryas) milk proteins
AU - Hall, A. J.
AU - Masel, A.
AU - Bell, K.
AU - Halliday, J. A.
AU - Shaw, D. C.
AU - Vandeberg, J. L.
N1 - Funding Information:
This work was supported by grants from the Australian Stud Book, Alison Road, Randwick, New South Wales, 2031, Australia, and the National Institutes of Health (Grant P51 RR13986 to the Southwest Regional Primate Research Center). Thanks are due to Mrs. M. Aivaliotis and the staff of the Veterinary Services Group of the Southwest Foundation Department of Physiology and Medicine for collecting the milk and tissue samples.
PY - 2001
Y1 - 2001
N2 - The major proteins of baboon milk were identified as β-lactoglobulin (βLG), α-lactalbumin (αLA), lysozyme, lactoferrin, casein, and albumin by immobiline isoelectric focusing, SDS-PAGE, immunoblotting of gels with rabbit antisera to human αLA, lysozyme, and albumin and bovine βLG and casein, and N-terminal sequencing of proteins blotted from gels. The first 30 N-terminal residues of baboon βLG are identical to those of macaque (Macaca fasicularis) βLG except for a (D/N) polymorphism at residue 2. The complete cDNA sequence and derived amino acid composition of βLG were elucidated using RT-PCR amplification of poly(A)+ mRNA purified from lactating mammary gland. Baboon βLG consists of 168 amino acid residues (Mr 20, 750) and is the longest βLG identified to date. βLG and αLA polymorphisms with three (A, B, and C) and two (A and B) variants, respectively, were detected by immobiline IEF, pH 4-6, of individual baboon milk samples at varying stages of lactation.
AB - The major proteins of baboon milk were identified as β-lactoglobulin (βLG), α-lactalbumin (αLA), lysozyme, lactoferrin, casein, and albumin by immobiline isoelectric focusing, SDS-PAGE, immunoblotting of gels with rabbit antisera to human αLA, lysozyme, and albumin and bovine βLG and casein, and N-terminal sequencing of proteins blotted from gels. The first 30 N-terminal residues of baboon βLG are identical to those of macaque (Macaca fasicularis) βLG except for a (D/N) polymorphism at residue 2. The complete cDNA sequence and derived amino acid composition of βLG were elucidated using RT-PCR amplification of poly(A)+ mRNA purified from lactating mammary gland. Baboon βLG consists of 168 amino acid residues (Mr 20, 750) and is the longest βLG identified to date. βLG and αLA polymorphisms with three (A, B, and C) and two (A and B) variants, respectively, were detected by immobiline IEF, pH 4-6, of individual baboon milk samples at varying stages of lactation.
KW - Baboon
KW - Milk
KW - Polymorphism
KW - cDNA
KW - β-lactoglobulin
UR - http://www.scopus.com/inward/record.url?scp=0034972338&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034972338&partnerID=8YFLogxK
U2 - 10.1023/A:1002749303252
DO - 10.1023/A:1002749303252
M3 - Article
C2 - 11444021
AN - SCOPUS:0034972338
SN - 0006-2928
VL - 39
SP - 59
EP - 71
JO - Biochemical Genetics
JF - Biochemical Genetics
IS - 1-2
ER -