Isolation and characterization of an enkephalin-hydrolyzing dipeptidyl-aminopeptidase from calf-brain striatum
Cytosolic dipeptidyl-aminopeptidase with a high affinity for Leu-enkephalin (K m = 5–7 μM) was partially purified from the 25,000 g supernatant of calf-brain striatum. The procedure included pH 4.5 denaturation, DEAE-cellulose chromatography and Blue Sepharose CL-6B chromatography and resulted in pr...
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| Veröffentlicht in: | Neuropeptides (Edinburgh) 1985-01, Vol.6 (5), p.381-389 |
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| creator | van Buuren, K.J.H. van Amsterdam, J.G.C. Mulder, J.R.A. Soudijn, W. |
| description | Cytosolic dipeptidyl-aminopeptidase with a high affinity for Leu-enkephalin (K
m = 5–7 μM) was partially purified from the 25,000 g supernatant of calf-brain striatum. The procedure included pH 4.5 denaturation, DEAE-cellulose chromatography and Blue Sepharose CL-6B chromatography and resulted in preparations that are free from other enkephalin-hydrolyzing enzymes. This enzyme, which is called enkephalinase B, has a positively charged group in its active site and presumably also a Zn atom since the loss in activity induced by EDTA treatment can be restored without loss of substrate affinity by low concentrations of ZnSO
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| doi_str_mv | 10.1016/0143-4179(85)90136-2 |
| format | Article |
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m = 5–7 μM) was partially purified from the 25,000 g supernatant of calf-brain striatum. The procedure included pH 4.5 denaturation, DEAE-cellulose chromatography and Blue Sepharose CL-6B chromatography and resulted in preparations that are free from other enkephalin-hydrolyzing enzymes. This enzyme, which is called enkephalinase B, has a positively charged group in its active site and presumably also a Zn atom since the loss in activity induced by EDTA treatment can be restored without loss of substrate affinity by low concentrations of ZnSO
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m = 5–7 μM) was partially purified from the 25,000 g supernatant of calf-brain striatum. The procedure included pH 4.5 denaturation, DEAE-cellulose chromatography and Blue Sepharose CL-6B chromatography and resulted in preparations that are free from other enkephalin-hydrolyzing enzymes. This enzyme, which is called enkephalinase B, has a positively charged group in its active site and presumably also a Zn atom since the loss in activity induced by EDTA treatment can be restored without loss of substrate affinity by low concentrations of ZnSO
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m = 5–7 μM) was partially purified from the 25,000 g supernatant of calf-brain striatum. The procedure included pH 4.5 denaturation, DEAE-cellulose chromatography and Blue Sepharose CL-6B chromatography and resulted in preparations that are free from other enkephalin-hydrolyzing enzymes. This enzyme, which is called enkephalinase B, has a positively charged group in its active site and presumably also a Zn atom since the loss in activity induced by EDTA treatment can be restored without loss of substrate affinity by low concentrations of ZnSO
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| subjects | Analytical, structural and metabolic biochemistry Animals Apoenzymes - analysis Biological and medical sciences Cattle Chromatography, DEAE-Cellulose Corpus Striatum - enzymology Cytosol - enzymology Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - analysis Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - isolation & purification Endopeptidases - analysis Enkephalins - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Hydrolysis Kinetics Metals - analysis Substrate Specificity |
| title | Isolation and characterization of an enkephalin-hydrolyzing dipeptidyl-aminopeptidase from calf-brain striatum |
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