Biomaterial Database

Studies on the structural basis of the heterogeneity of human prostatic and seminal acid phosphatases. 1983

E M Taga, and D L Moore, and R L Van Etten

We studied possible causes of the electrophoretic heterogeneity of the acid phosphatase (EC 3.1.3.2) purified by affinity chromatography from human prostate and human seminal fluid. The isoelectric focusing pattern in polyacrylamide gel shows numerous bands in the pH range 4.0-5.2 and 5.5-5.9. Treatment with neuraminidase under conditions shown to cause complete removal of sialic acid does not abolish the observed heterogeneity. Although there is a change of the more acidic forms to ones having more basic pI values, at least 4 distinct bands remain. Structural differences at the amino terminal end can be ruled out as the cause of the remaining electrophoretic heterogeneity. Lysine is shown to be the amino terminal amino acid for both the prostatic and seminal fluid enzymes. The sequences of the first 23 amino acids are shown to be identical for the prostatic and seminal fluid acid phosphatases. The functional enzyme contains no metal ion but it can be stoichiometrically inactivated by cupric ion.

UI	MeSH Term	Description	Entries
D007525	Isoelectric Focusing	Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.	Electrofocusing,Focusing, Isoelectric
D007527	Isoenzymes	Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.	Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008297	Male		Males
D009439	Neuraminidase	An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)	Sialidase,Exo-alpha-Sialidase,N-Acylneuraminate Glycohydrolases,Oligosaccharide Sialidase,Exo alpha Sialidase,Glycohydrolases, N-Acylneuraminate,N Acylneuraminate Glycohydrolases,Sialidase, Oligosaccharide
D011467	Prostate	A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM.	Prostates
D002621	Chemistry	A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000135	Acid Phosphatase	An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.	Acid beta-Glycerophosphatase,Acid beta Glycerophosphatase
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein