Results 61 to 70 of about 347 (91)

Bioaugmentation and vermicompost facilitated the hydrocarbon bioremediation: scaling up from lab to field for petroleum-contaminated soils. [PDF]

Environ Sci Pollut Res Int
Curiel-Alegre S, Khan AHA, Rad C, Velasco-Arroyo B, Rumbo C, Rivilla R, Durán D, Redondo-Nieto M, Borràs E, Molognoni D, Martín-Castellote S, Juez B, Barros R.   +12 more
europepmc   +1 more source

Structure-guided discovery of aminopeptidase ERAP1 variants capable of processing antigens with novel PC anchor specificities. [PDF]

Immunology
Pande S, Guo HC.
europepmc   +1 more source

Bee pollen peptides as potent tyrosinase inhibitors with anti-melanogenesis effects in murine b16f10 melanoma cells and zebrafish embryos. [PDF]

Sci Rep
Sangtanoo P, Srimongkol P, Saisavoey T, Puthong S, Buakeaw A, Suttisuwan R, Jatupornpipat M, Pimtong W, Reamtong O, Karnchanatat A.   +9 more
europepmc   +1 more source

Pectin supplementation accelerates post-antibiotic gut microbiome reconstitution orchestrated with reduced gut redox potential. [PDF]

ISME J
Xu R, Feng N, Li Q, Wang H, Li L, Feng X, Su Y, Zhu W.   +7 more
europepmc   +1 more source

Microbial remineralization processes during postspring-bloom with excess phosphate available in the northern Baltic Sea. [PDF]

FEMS Microbiol Ecol
Vanharanta M, Santoro M, Villena-Alemany C, Piiparinen J, Piwosz K, Grossart HP, Labrenz M, Spilling K.   +7 more
europepmc   +1 more source

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Identification of Cytosolic Leucyl Aminopeptidase (EC 3.4.11.1) as the Major Cysteinylglycine-Hydrolysing Activity in Rat Liver

Biological Chemistry, 2003
Cysteinylglycine hydrolysis is a step in the metabolism of glutathione and glutathione S-conjugates. We had previously observed that in rat liver the enzymatic activity is predominantly located in the cytosol. Here we demonstrate that cytosolic leucyl aminopeptidase (EC 3.4.11.1) is the major cysteinylglycine hydrolysing activity in rat liver. Evidence
Claudio, Jösch, Lars-Oliver, Klotz, Helmut, Sies   +2 more
openaire   +2 more sources

Purification, preliminary characterization, and immunological comparison of hog lens leucine aminopeptidase (EC 3.4.11.1) with hog kidney and beef lens aminopeptidases

Analytical Biochemistry, 1985
Leucine aminopeptidase (LAP) was purified from hog lenses by application of the Himmelhoch procedure for isolation of hog kidney LAP [S. R. Himmelhoch (1970) in Methods in Enzymology (Perlmann, G. E., and Lorand, L., eds.), Vol. 19, pp. 508-513, Academic Press, New York.] This involved treating crude hog lens homogenates with hexadecyltrimethylammonium
H C, Oettgen, A, Taylor
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[42] Crystalline leucine aminopeptidase from lens (α-aminoacyl-peptide hydrolase; EC 3.4.11.1)

1976
Publisher Summary Leucine aminopeptidase (LAP) is a Zn-enzyme localized in the cytosol and occurring in the tissues and body fluids of all organisms. LAP, crystallized at first from bovine eye lens, TM shows a total or partial immunological identity in different tissues of vertebrates (liver, kidney) and also in different vertebrate species ...
Horst Hanson, Marlies Frohne
openaire   +1 more source

Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce, Lorenzo Cohen, Karen M Mustian   +2 more
exaly