[Separation and properties of multiple forms of acid phosphatase from the tissues and organs of the mulberry silkworm].
The multiple forms of acid phosphatase from the hemolymph, fat body, intestinal wall and silk gland of the silkworm larvae differing in their mobility during polyacrylamide gel electrophoresis were separated by isoelectrofocusing, gel filtration and ion-exchange chromatography and characterized in terms of their molecular weight, isoelectric points and substrate specificity. It was found that silkworm tissues contain several enzyme forms possessing broad substrate specificity (EC 3.1.3.2) as well as forms predominantly catalyzing the hydrolysis of glucose-1-phosphate (EC 3.1.3.10). The enzyme forms with a broad substrate specificity were detected in all tissues studied with the exception of hemolymph and were found to have the molecular weights above 60,000, pI greater than pH 6.0 and the highest activity within the pH range of 3.0-4.5. The enzyme forms causing predominant hydrolysis of glucose-1-phosphate detected in the hemolymph, fat body and intestinal wall are characterized by Mr = 30,000-100,000, pI below 6.0 and the highest activity within the pH range of 4.8-5.6. A possible role of the multiple forms of acid phosphatase in silkworm metabolism is discussed.
D000135:Acid Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity; D014018:Tissue Distribution
D007527:Isoenzymes; D000135:Acid Phosphatase
Razdelenie i svoĭstva mnozhestvennykh form kisloĭ fosfatazy tkaneĭ i organov tutovogo shelkopriada.