Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Keiko, Yamafuji"'
Publikováno v:
Nutrition and Metabolic Insights, Vol 2009, Iss 2, Pp 17-25 (2009)
Externí odkaz:
https://doaj.org/article/7b8a545829a9469392f0fa32761fab7d
Publikováno v:
Nutrition and Metabolic Insights, Vol 2009, Iss 2, Pp 17-25 (2009)
Nutrition and Metabolic Insights, Vol 2 (2009)
Nutrition and Metabolic Insights, Vol 2 (2009)
Background/AimsWe have previously isolated a novel lysosomal cysteine protease, cathepsin Y, which produces a kinin-potenciating octapeptide from rat plasma. The present study aimed to elucidate the influence of protein-restriction on cathepsin Y mRN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e3568a98c5e38e3bd4a1e6f6b9d85d
http://www.la-press.com/cathepsin-y-expression-is-up-regulated-in-liver-and-spleen-of-the-rats-a1448
http://www.la-press.com/cathepsin-y-expression-is-up-regulated-in-liver-and-spleen-of-the-rats-a1448
Publikováno v:
Biological chemistry. 383(12)
A cysteine endopeptidase from rat spleen was purified, characterized and its gene cloned. This enzyme was originally recognized by its action of producing kinin-potentiating peptide from a plasma protein. We named it cathepsin Y due to its localizati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dd58a991c5b7811ff0b1975b60326bba
https://pubmed.ncbi.nlm.nih.gov/12553736
https://pubmed.ncbi.nlm.nih.gov/12553736
Publikováno v:
Biological Chemistry. 383
A cysteine endopeptidase from rat spleen was purified, characterized and its gene cloned. This enzyme was originally recognized by its action of producing kinin-potentiating peptide from a plasma protein. We named it cathepsin Y due to its localizati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f128a2a862382c032e85049b68d8f391
https://doi.org/10.1515/bc.2002.223
https://doi.org/10.1515/bc.2002.223
Publikováno v:
Immunopharmacology. 45(1-3)
Rat spleen cathepsin Y (a novel enzyme) that produces bradykinin (BK) potentiating peptide (BPP) from rat plasma was isolated, characterized and its amino acid sequence was deduced from cDNA cloned by reverse transcription-polymerase chain reaction (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eed338180631c191a76800d4aaf68ca9
https://pubmed.ncbi.nlm.nih.gov/10615013
https://pubmed.ncbi.nlm.nih.gov/10615013
Publikováno v:
Immunopharmacology. 32(1-3)
We have focused our studies on a thiol-dependent enzyme of 37 kilodaltons (kDa) that produces a bradykinin (BK) potentiating peptide. The molecular mass of the peptide was estimated to be around 750 Da and its amino acid composition was Pro 4 Gly 2 L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b93fb26f54b1170162509600f144e96
https://pubmed.ncbi.nlm.nih.gov/8796296
https://pubmed.ncbi.nlm.nih.gov/8796296
Autor:
Lowell M. Greenbaum, Keiko Yamafuji
Publikováno v:
Life Sciences. 4:657-663
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::226f6b9cf62a585c120987138a76c865
https://doi.org/10.1016/0024-3205(65)90004-4
https://doi.org/10.1016/0024-3205(65)90004-4
Autor:
Keiko Yamafuji, Masako Watanabe
Publikováno v:
Kinins IV ISBN: 9781468451450
Intracellular distributions of acid kininogenases were investigated following the subcellular fractionation of bovine and rat spleens. Acid kininogenases as well as other acid hydrolases were observed to be distributed in several fractons. Relatively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca759b6cb04d9d3869fe029c809acd05
https://doi.org/10.1007/978-1-4684-5143-6_3
https://doi.org/10.1007/978-1-4684-5143-6_3
Autor:
Makiko Takeishi, Keiko Yamafuji
Publikováno v:
Kinins—II ISBN: 9781475709285
Two kinin forming enzymes were extracted. from bovine spleen and separated from cathepsin Bl and B2 by DEAE-Cellulose chromatography. Since these catheptic kininogenases were found to release kinins from kininogens at acidic pH’s, these were named
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fdbb63510b27dd46f19080cac2225776
https://doi.org/10.1007/978-1-4757-0926-1_32
https://doi.org/10.1007/978-1-4757-0926-1_32
Autor:
Keiko Yamafuji, Lowell M. Greenbaum
Publikováno v:
Hypotensive Peptides ISBN: 9783642949678
For several years our laboratory has been concerned with the properties and possible functions of the intracellular proteinases known as the cathepsins. These enzymes exist in the lysosomal particles of the cell (de Duve, 1959) and consist of a serie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3b2e69be9ae2145b66f8f2dc7469b3f
https://doi.org/10.1007/978-3-642-94965-4_24
https://doi.org/10.1007/978-3-642-94965-4_24