Tissue specificities of protease A-like esteroprotease in male mice.
An esteroprotease hydrolyzing p-tosyl-L-arginine methyl ester (TAME) has been purified to homogeneity from male mice submandibular glands by the ammonium sulphate precipitation, Sephadex gel chromatography and DEAE-cellulose chromatography. The enzyme was shown as a single chain acidic protein (pI = 5.7) with the molecular weight of 27.5 K and evidence was obtained to reveal that it was similar to protease A. Using this enzyme as antigen we prepared anti-TAMEase antibody. The immunoblotting studies on tissue specificity using 20 different tissues from male mice revealed that cross-reactivities with anti-TAMEase antibody were observed in the crude extract from the sublingual gland, parotid gland and pancreas. The species specificity studies with the submandibular glands of 7 different species indicated that only the crude extract from rat submandibular glands reacted against anti-TAMEase antibody but it exerted a low TAMEase activity.
Kurokawa
R
R
Department of Biochemistry, Iwate Medical University School of Dentistry, Japan.
Baba
R
R
Ota
M
M
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D016282:Aspartic Acid Endopeptidases; D003429:Cross Reactions; D010450:Endopeptidases; D005260:Female; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013363:Submandibular Gland / Q000201:enzymology*; D014018:Tissue Distribution
D000906:Antibodies; D010450:Endopeptidases; D010447:Peptide Hydrolases; C023073:tosylarginine methyl ester hydrolase; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases