Zobrazeno 1 - 7 of 7 pro vyhledávání: '"H L Jackman"'
1
Dominant chymotrypsin-like esterase activity in human lymphocyte granules is mediated by the serine carboxypeptidase called cathepsin A-like protective protein
Autor: W L Hanna, J M Turbov, H L Jackman, F Tan, C J Froelich
Publikováno v: The Journal of Immunology. 153:4663-4672
We identified a chymotrypsin-like activity in the granules of IL-2 lymphokine-activated killer (LAK) cells and a NK cell line (YT) that reacted preferentially with the oligopeptide substrate succinyl-Phe-Leu-Phe-thiobenzyl ester (Suc-Phe-Leu-Phe-SBzl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80d0aa2bc24eb6cf983b1d257564b8ea
https://doi.org/10.4049/jimmunol.153.10.4663
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2
Single-domain angiotensin I converting enzyme (kininase II): characterization and properties
Autor: P A, Deddish, L X, Wang, H L, Jackman, B, Michel, J, Wang, R A, Skidgel, E G, Erdös
Publikováno v: The Journal of pharmacology and experimental therapeutics. 279(3)
Somatic angiotensin I converting enzyme (ACE; kininase II) has two active sites, in two (N and C) domains. We studied the active centers with separate N-domain ACE (N-ACE), testicular C-domain ACE (germinal ACE) and, as control, renal somatic ACE. Ge
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::13d850876af5d27b3e2a5e577df08f44
https://pubmed.ncbi.nlm.nih.gov/8968386
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3
Dominant chymotrypsin-like esterase activity in human lymphocyte granules is mediated by the serine carboxypeptidase called cathepsin A-like protective protein
Autor: W L, Hanna, J M, Turbov, H L, Jackman, F, Tan, C J, Froelich
Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 153(10)
We identified a chymotrypsin-like activity in the granules of IL-2 lymphokine-activated killer (LAK) cells and a NK cell line (YT) that reacted preferentially with the oligopeptide substrate succinyl-Phe-Leu-Phe-thiobenzyl ester (Suc-Phe-Leu-Phe-SBzl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8907c29b6b00fb8013e24d03c4878936
https://pubmed.ncbi.nlm.nih.gov/7963538
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4
Inactivation of endothelin I by deamidase (lysosomal protective protein)
Autor: H L, Jackman, P W, Morris, P A, Deddish, R A, Skidgel, E G, Erdös
Publikováno v: The Journal of biological chemistry. 267(5)
Deamidase cleaves ester and peptide bonds in various substrates and deamidates protected COOH-terminal amino acids. It preferentially hydrolyzes peptides which contain hydrophobic amino acids in the P1' and/or P1 position. Because the COOH-terminal e
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ef79cf7a0e7a1250fcee40d55014e0f6
https://pubmed.ncbi.nlm.nih.gov/1737744
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5
A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal 'protective protein'
Autor: H L, Jackman, F L, Tan, H, Tamei, C, Beurling-Harbury, X Y, Li, R A, Skidgel, E G, Erdös
Publikováno v: The Journal of biological chemistry. 265(19)
We discovered an enzyme in human platelets that deamidates substance P and other tachykinins. Because an amidated carboxyl terminus is important for biological activity, we purified and characterized this deamidase. The enzyme, released from human pl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fb7ae1a2b641228cd9eb57771866a140
https://pubmed.ncbi.nlm.nih.gov/1694176
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