Investigation of the heterogeneity of rhesus monkey alpha 1-antitrypsin.
Rhesus monkey alpha 1-antitrypsin (n = 144) was examined for heterogeneity by acid starch gel electrophoresis, isoelectric focusing in agarose and agarose gel electrophoresis. In contrast to other studies, no heterogeneity of Rhesus monkey alpha 1-antitrypsin could be documented using specific antisera. Rhesus monkey alpha 1-antitrypsin contained a reactive thiol. The pIs of the major isoforms of Rhesus monkey alpha 1-antitrypsin were 4.63, 4.69, 4.84 and 4.86 at 4 degrees C. No deficiency state of Rhesus monkey alpha 1-antitrypsin was detected. The six protease inhibitors in Rhesus monkey sera cross-reacted with antisera to the six human protease inhibitors.
D000818:Animals; D000936:Antigen-Antibody Complex; D003429:Cross Reactions; D004587:Electrophoresis, Agar Gel; D004592:Electrophoresis, Starch Gel; D007106:Immune Sera; D007525:Isoelectric Focusing; D008253:Macaca mulatta; D010447:Peptide Hydrolases / Q000097:blood / Q000276:immunology; D000515:alpha 1-Antitrypsin / Q000276:immunology / Q000302:isolation & purification*
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D000515:alpha 1-Antitrypsin; D010447:Peptide Hydrolases