Results 241 to 250 of about 180,264 (297)

Lysosomal hydrolases of the epidermis.

British Journal of Dermatology, 1975
Four distinct peptide hydrolases (EC 3-4) have been characterized in guinea-pig epidermis; these are cathepsin B1, cathepsin C, cathepsin D and arylamidase. Their properties are consistent with those of lysosomal enzymes. Cathepsin E was not detected.
P D, Mier, J J, van den Hurk
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Leukotriene A4 hydrolase: An epoxide hydrolase with peptidase activity

Biochemical and Biophysical Research Communications, 1990
Purified leukotriene A4 hydrolase from human leukocytes is shown to exhibit peptidase activity towards the synthetic substrates alanine-4-nitroanilide and leucine-4-nitroanilide. The enzymatic activity is abolished after heat treatment (70 degrees C, 30 min).
J Z, Haeggström, A, Wetterholm, B L, Vallee, B, Samuelsson   +3 more
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Cytosolic epoxide hydrolase

Chemico-Biological Interactions, 1988
Epoxide hydrolase activity is recovered in the high-speed supernatant fraction from the liver of all mammals so far examined, including man. For some as yet unexplained reason, the rat has a very low level of this activity, so that cytosolic epoxide hydrolase is generally studied in mice.
Joseph W Depierre, J W Depierre, Johan Meijer   +2 more
exaly   +3 more sources

Endocannabinoid hydrolases

Prostaglandins & Other Lipid Mediators, 2002
Endocannabinoids (endogenous ligands of cannabinoid receptors) such as anandamide (N-arachidonoylethanolamine) and 2-arachidonoylglycerol (2-AG) are inactivated upon enzymatic hydrolysis. Recent progress in the enzymological and molecular biological studies on the 'endocannabinoid hydrolases' is reviewed in this article.
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ADP-ribosylarginine hydrolases

Molecular and Cellular Biochemistry, 1994
ADP-ribosylation is a reversible post-translational modification of proteins involving the addition of the ADP-ribose moiety of NAD to an acceptor protein or amino acid. NAD:arginine ADP-ribosyltransferase, purified from numerous animal tissues, catalyzes the transfer of ADP-ribose to an arginine residue in proteins.
T, Takada, I J, Okazaki, J, Moss
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Extracellular hydrolases of the lung

Biochemistry, 1978
A pool of acid hydrolases exists within the acellular lining material of the alveoli and distal airways of the lungs. These extracellular hydrolases, obtained using pulmonary lavage procedures, appear to be of a selected variety insofar as some hydrolases (beta-N-acetylglucosaminidase and alpha-mannosidase) are highly active while others (beta ...
Gary E. R. Hook, Linda B. Gilmore
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Leukotriene A4 hydrolase

Prostaglandins & Other Lipid Mediators, 2002
The leukotrienes (LTs) are a family of lipid mediators involved in inflammation and allergy. Leukotriene B4 is a classical chemoattractant, which triggers adherence and aggregation of leukocytes to the endothelium at only nanomolar concentrations.
Jesper Z, Haeggström, Filippa, Kull, Peter C, Rudberg, Fredrik, Tholander, Marjolein M G M, Thunnissen   +4 more
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Endo-Xylogalacturonan Hydrolase

2003
Commercial pectinases used in apple juice manufacturing contain a mixture of pectin-degrading enzyme activities. Nevertheless, fragments of branched pectic molecules (or pectic hairy regions) are resistant to degradation, and can cause membrane fouling in the final ultrafiltration step of concentrated apple juice.
Herweijer, M.A., Vincken, J.P., Meeuwsen, P.J.A., van der Vlugt-Bergmans, C.J.B., Beldman, G., van Ooyen, A.J.J., Voragen, A.G.J.   +6 more
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Dimetallic hydrolases and their models

Current Opinion in Chemical Biology, 2000
Recent mechanistic studies of Fe3+/M2+ purple acid phosphatase present conflicting pictures about the roles of the metals. Recent model studies with Co3+/Co3+ and Fe3+/Fe3+ complexes have supported each conflicting mechanism for phosphate hydrolysis.
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Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Partial amino acid sequence of 80 kDa oxidized protein hydrolase (OPH), a serine protease present in human erythrocyte cytosol (Fujino et al., J. Biochem. 124 (1998) 1077-1085) that is adherent to oxidized erythrocyte membranes and preferentially degrades oxidatively damaged proteins (Beppu et al., Biochim. Biophys. Acta 1196 (1994) 81-87; Fujino et al.
T, Fujino, K, Watanabe, M, Beppu, K, Kikugawa, H, Yasuda   +4 more
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