Phosphorylation of different human milk proteins by human catalytic secretory immunoglobulin A.
The ability of secretory immunoglobulin A (slgA) from milk of healthy mothers to phosphorylate various milk proteins in the presence of gamma-[32P]-ATP was shown to be a property of the antibodies. The polyclonal slgA was purified by sequential chromatography on Protein-A Sepharose and DEAE-cellulose, and then separated by chromatography on the ATP-Sepharose. The preparations containing all milk proteins except for protein kinases [integrated milk proteins (IMP)] were obtained by extraction of the kinase activities from the milk using their affinity to the insoluble crosslinked staphylococcus. Addition of slgA fractions (having a different affinity to ATP) to the IMP led to phosphorylation of casein and several other milk proteins with different efficiencies.
Kit YYa
Novosibirsk Institute of Bioorganic Chemistry, Academy of Sciences, Russia.
Semenov
D V
DV
Nevinsky
G A
GA
D000255:Adenosine Triphosphate / Q000378:metabolism; D017151:Antibodies, Catalytic / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003636:DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007071:Immunoglobulin A, Secretory / Q000302:isolation & purification / Q000494:pharmacology*; D008894:Milk Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D017151:Antibodies, Catalytic; D002364:Caseins; D007071:Immunoglobulin A, Secretory; D008894:Milk Proteins; D000255:Adenosine Triphosphate; D003636:DEAE-Cellulose; D011494:Protein Kinases; D014357:Trypsin