The isolation and some properties of dipeptidyl peptidases II and III from porcine spleen.
1. Dipeptidyl peptidases (DPP) II and III from porcine spleen have been purified to homogeneity as assessed by disc gel electrophoresis, HPLC and chromatofocusing. 2. The enzyme are both inhibited by diisopropylfluorophosphate suggesting that the active site contains an essential serine residue, but they are also inhibited by a variety of other reagents. 3. The pI of DPP II is 4.8, that of DPP III, 4.0. 4. The former enzyme has a molecular weight of 97,000, the latter 66,000 and both are glycoproteins. 5. The enzymes are compared with those from other sources.
Lynn
K R
KR
Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007531:Isoflurophate / Q000494:pharmacology; D008970:Molecular Weight; D013057:Spectrum Analysis; D013154:Spleen / Q000201:enzymology*; D013552:Swine
D000596:Amino Acids; D007531:Isoflurophate; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100151:dipeptidyl peptidase II; C100152:dipeptidyl peptidase III