3.4.23.25	additional information	-	a precursor of MW 52000 is processed to the mature form of 42000 MW	30698	
3.4.23.25	additional information	-	homology to: mammalian aspartyl proteases such as pepsin, renin and cathepsin	30696	
3.4.23.25	additional information	-	partial primary structure	30702	
3.4.23.25	additional information	-	primary structure	30712	
3.4.23.25	additional information	-	proteinase A is synthesized as a 405-amino-acid precursor which is proteolytically converted to the 329-amino-acid mature enzyme	30696	
3.4.23.25	40760	-	laser desorption mass spectroscopy, a second form with MW 38132 isolated from the culture medium is an underglycosylated form lacking the carbohydrate moiety at Asn269	30705	
3.4.23.25	41400	-	sedimentation-diffusion equilibrium ultracentrifugation	30697	
3.4.23.25	41700	-	1 * 41700, Saccharomyces cerevisiae, SDS-PAGE	30697	
3.4.23.25	42000	-	-	652836	
3.4.23.25	42000	-	1 * 42000, Saccharomyces cerevisiae, SDS-PAGE	30705	
3.4.23.25	42000	-	1 * 42000, SDS-PAGE, native mass by gel filtration	683560	
3.4.23.25	42000	-	enzyme form A', gel filtration	30710	
3.4.23.25	43000	-	-	649129	
3.4.23.25	45000	-	1 * 45000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE	30710	
3.4.23.25	45000	-	gel filtration	30709	
3.4.23.25	49000	-	enzyme form A, gel filtration	30710	
3.4.23.25	54000	-	1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE	30710	
3.4.23.25	55000	-	gel filtration	683560