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Bovine spleen acid kininogenases
Conference Abstracts
82 2
2. 3. 4.
Vol. 16, No . 5
Actions 3 332 (1973) .
N . BACR and R . STEGER, Prop . Soc. Etp. Siol . Med. Z4 3 769 (1973) . H .Z . MOVAT, S .G . STEINBERG, F .M . PABAL and N.S . aANADIVE, Lab . Investigation 29 669 (1973) . A.M . ROTHSCHILD, R.S .B . CORDEIRO and A. CASTANIA, Naunyn-Sc3nmiedebergs Arch. Phaxgrakol . 282 323 (1974) . BOVINE SPLEEN ACID KININOGENASES Keiko Yamafuju and Makiko Takeishi
Department of Biochemistry, Nakamura Gakuen College, Fukuoka, Japan Rininogenase and Kininase activities have been found in cathepain B preparations of spleen . The kininogeaasea were differentiated by ion exchange chromatography on DEAE-cellulose . An SH independent and SH dependent kininogen ase were separated from cathepain B1 . Since the kininogenasea are active at acidic conditions, the authors propose to call them acid kininogenase I and II (in order of elution) . The active peptide formed by kininogenase I has a molecuThe rat uterus contracting aclar weight of 1,300 and N-terminal methionine . tivity was increased three times when the peptide was incubated with trypain Thus the and diminished when treated with chymotrypain or pancreatic cease B. peptide probably should be assigned the structure of Met-Lys-Bradykinin . The enzyme preparation from DEAF-cellulose was subjected to ion exchange chromatography on TEAS-cellulose and affinity chromatography on hemoglobin-sepharose 4B . From the assay of the enzyme activity and the molecular weight determination of the components (by S.D .S . gel electrophoresis at each step of purification), the relationships between protein composition and tha enzyme activities were deduced. The component of M.W . 24,000 is essential for SH independent kininoThe genase activity, whereas 27,000 is for SH dependent kininogenase activity . allosteric effects of these and the other components and the mechanism of their transitions remain to be elucidated . ROLE OF THE RALLIKREIN-KININ SYSTEM IN INFLAMMATION C .G . Van Armar Merck Institute for Therapeutic Research, Weat Point, Pennsylvania Inflammations may be acute or chronic and the mechanisms may differ greatly with either type . In certain acute laboratory models and in the initial stages of certain naturally-occurring diseases, cellular elements are apparently not necessary for the inflammatory process to begin . The kallikrein-kinin system here may play an important role . Kinine~probably help to trigger the events that come later. Bradykinin, proataglandina, and serotonin potentiate each other's short-term inflammatory effects, as measured by pain and swelling . The question is not yet settled whether kinine may have a more important role in inflammation than merely helping to initigte it . It seems not likely at present that bradykinln, serotonin, prostaglandins, and histamine, all taken together, can account for all of the rat's foot swelling caused by carrageenan . Carboaypeptidase B, which destroys bradykinin, reduces somewhat an acute inflammation in the rat's foot by carrageenan, but does not reduce a similar inflammation in the dog's knee joint . Although it may seem unlikely quantitatively, still, if pros8aglandins and bradykinin could be produced at a local site in
82 2
2. 3. 4.
Vol. 16, No . 5
Actions 3 332 (1973) .
N . BACR and R . STEGER, Prop . Soc. Etp. Siol . Med. Z4 3 769 (1973) . H .Z . MOVAT, S .G . STEINBERG, F .M . PABAL and N.S . aANADIVE, Lab . Investigation 29 669 (1973) . A.M . ROTHSCHILD, R.S .B . CORDEIRO and A. CASTANIA, Naunyn-Sc3nmiedebergs Arch. Phaxgrakol . 282 323 (1974) . BOVINE SPLEEN ACID KININOGENASES Keiko Yamafuju and Makiko Takeishi
Department of Biochemistry, Nakamura Gakuen College, Fukuoka, Japan Rininogenase and Kininase activities have been found in cathepain B preparations of spleen . The kininogeaasea were differentiated by ion exchange chromatography on DEAE-cellulose . An SH independent and SH dependent kininogen ase were separated from cathepain B1 . Since the kininogenasea are active at acidic conditions, the authors propose to call them acid kininogenase I and II (in order of elution) . The active peptide formed by kininogenase I has a molecuThe rat uterus contracting aclar weight of 1,300 and N-terminal methionine . tivity was increased three times when the peptide was incubated with trypain Thus the and diminished when treated with chymotrypain or pancreatic cease B. peptide probably should be assigned the structure of Met-Lys-Bradykinin . The enzyme preparation from DEAF-cellulose was subjected to ion exchange chromatography on TEAS-cellulose and affinity chromatography on hemoglobin-sepharose 4B . From the assay of the enzyme activity and the molecular weight determination of the components (by S.D .S . gel electrophoresis at each step of purification), the relationships between protein composition and tha enzyme activities were deduced. The component of M.W . 24,000 is essential for SH independent kininoThe genase activity, whereas 27,000 is for SH dependent kininogenase activity . allosteric effects of these and the other components and the mechanism of their transitions remain to be elucidated . ROLE OF THE RALLIKREIN-KININ SYSTEM IN INFLAMMATION C .G . Van Armar Merck Institute for Therapeutic Research, Weat Point, Pennsylvania Inflammations may be acute or chronic and the mechanisms may differ greatly with either type . In certain acute laboratory models and in the initial stages of certain naturally-occurring diseases, cellular elements are apparently not necessary for the inflammatory process to begin . The kallikrein-kinin system here may play an important role . Kinine~probably help to trigger the events that come later. Bradykinin, proataglandina, and serotonin potentiate each other's short-term inflammatory effects, as measured by pain and swelling . The question is not yet settled whether kinine may have a more important role in inflammation than merely helping to initigte it . It seems not likely at present that bradykinln, serotonin, prostaglandins, and histamine, all taken together, can account for all of the rat's foot swelling caused by carrageenan . Carboaypeptidase B, which destroys bradykinin, reduces somewhat an acute inflammation in the rat's foot by carrageenan, but does not reduce a similar inflammation in the dog's knee joint . Although it may seem unlikely quantitatively, still, if pros8aglandins and bradykinin could be produced at a local site in