Partial purification and characterization of trehalase from axenically grown myxamoebae of Dictyostelium discoideum
Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase,...
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| Published in | Biochimica et biophysica acta Vol. 1035; no. 3; pp. 243 - 248 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
14.09.1990
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/0304-4165(90)90085-B |
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| Abstract | Lysosomal trehalase from the myxamoebae of
Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase, which is electrophoretically homogenous, appears as two peaks of activity when subjected to hydroxypatite and gel filtration chromatography. The enzyme has isoelectric points of 4.0 and < 2.5. Among natural disaccharides tested, the purified trehalase showed absolute specificity for trehalose with an apparent
K
m of 1.15 mM. However, the enzyme efficiently utilized the synthetic sugar α-
d-glucosyl fluoride as a substrate. Various methods were employed to estimate the apparent molecular weight, which was found to lie in the range of 30–162 kDa. |
|---|---|
| AbstractList | Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase, which is electrophoretically homogeneous, appears as two peaks of activity when subjected to hydroxyapatite and gel filtration chromatography. The enzyme has isoelectric points of 4.0 and less than 2.5. Among natural disaccharides tested, the purified trehalase showed absolute specificity for trehalose with an apparent Km of 1.15 mM. However, the enzyme efficiently utilized the synthetic sugar alpha-D-glucosyl fluoride as a substrate. Various methods were employed to estimate the apparent molecular weight, which was found to lie in the range of 30-162 kDa. Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase, which is electrophoretically homogeneous, appears as two peaks of activity when subjected to hydroxyapatite and gel filtration chromatography. The enzyme has isoelectric points of 4.0 and less than 2.5. Among natural disaccharides tested, the purified trehalase showed absolute specificity for trehalose with an apparent Km of 1.15 mM. However, the enzyme efficiently utilized the synthetic sugar alpha-D-glucosyl fluoride as a substrate. Various methods were employed to estimate the apparent molecular weight, which was found to lie in the range of 30-162 kDa.Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase, which is electrophoretically homogeneous, appears as two peaks of activity when subjected to hydroxyapatite and gel filtration chromatography. The enzyme has isoelectric points of 4.0 and less than 2.5. Among natural disaccharides tested, the purified trehalase showed absolute specificity for trehalose with an apparent Km of 1.15 mM. However, the enzyme efficiently utilized the synthetic sugar alpha-D-glucosyl fluoride as a substrate. Various methods were employed to estimate the apparent molecular weight, which was found to lie in the range of 30-162 kDa. Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and electrophoretic conditions reveals its close similarities to other lysosomal enzymes that have been studied earlier. The cellular trehalase, which is electrophoretically homogenous, appears as two peaks of activity when subjected to hydroxypatite and gel filtration chromatography. The enzyme has isoelectric points of 4.0 and < 2.5. Among natural disaccharides tested, the purified trehalase showed absolute specificity for trehalose with an apparent K m of 1.15 mM. However, the enzyme efficiently utilized the synthetic sugar α- d-glucosyl fluoride as a substrate. Various methods were employed to estimate the apparent molecular weight, which was found to lie in the range of 30–162 kDa. |
| Author | Gupta, Jyothi Cotter, David Allen |
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| Cites_doi | 10.1016/0003-9861(86)90067-6 10.1128/JB.103.2.375-381.1970 10.1042/bj0910222 10.1016/0003-2697(77)90111-7 10.1016/0003-9861(86)90122-0 10.1126/science.151.3709.454 10.1038/227680a0 10.1016/0147-5975(83)90076-2 10.1042/bj0960595 10.1111/j.1749-6632.1984.tb13898.x 10.1016/S0065-2318(08)60266-8 10.1021/bi00256a009 10.1007/BF01588179 10.1111/j.1749-6632.1964.tb14213.x 10.1016/S0300-9084(75)80276-8 10.1007/BF02358184 10.1016/0008-6215(86)85022-4 10.1016/S0076-6879(83)96069-X 10.1016/0147-5975(86)90039-3 10.1016/0003-2697(76)90527-3 10.1128/MMBR.48.1.42-59.1984 10.1016/0003-9861(83)90554-4 |
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| Keywords | Lysosomal enzmye D. discoideum Trehalase Glycoprotein |
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| Snippet | Lysosomal trehalase from the myxamoebae of
Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and... Lysosomal trehalase from the myxamoebae of Dictyostelium discoideum has been partially purified. The behavior of the enzyme under different chromatographic and... |
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| SubjectTerms | Chromatography Chromatography, DEAE-Cellulose Chromatography, Gel D. discoideum Dictyostelium - enzymology Dictyostelium - growth & development Durapatite Electrophoresis, Polyacrylamide Gel Glycoprotein Hydroxyapatites Kinetics Lysosomal enzmye Molecular Weight Trehalase Trehalase - isolation & purification Trehalase - metabolism |
| Title | Partial purification and characterization of trehalase from axenically grown myxamoebae of Dictyostelium discoideum |
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