Characterization of baboon (Papio hamadryas) milk proteins

A. J. Hall; A. Masel; K. Bell; J. A. Halliday; D. C. Shaw; J. L. Vandeberg

doi:10.1023/A:1002749303252

Characterization of baboon (Papio hamadryas) milk proteins

A. J. Hall, A. Masel, K. Bell^*, J. A. Halliday, D. C. Shaw, J. L. Vandeberg

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

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 (M_r 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.

Original language	English
Pages (from-to)	59-71
Number of pages	13
Journal	Biochemical Genetics
Volume	39
Issue number	1-2
DOIs	https://doi.org/10.1023/A:1002749303252
Publication status	Published - 2001

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title = "Characterization of baboon (Papio hamadryas) milk proteins",

abstract = "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.",

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author = "Hall, \{A. J.\} and A. Masel and K. Bell and Halliday, \{J. A.\} and Shaw, \{D. C.\} and Vandeberg, \{J. L.\}",

year = "2001",

doi = "10.1023/A:1002749303252",

language = "English",

volume = "39",

pages = "59--71",

journal = "Biochemical Genetics",

issn = "0006-2928",

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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.

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 - https://www.scopus.com/pages/publications/0034972338

U2 - 10.1023/A:1002749303252

DO - 10.1023/A:1002749303252

M3 - Article

SN - 0006-2928

VL - 39

SP - 59

EP - 71

JO - Biochemical Genetics

JF - Biochemical Genetics

IS - 1-2

ER -

Characterization of baboon (Papio hamadryas) milk proteins

Abstract

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