Results 11 to 20 of about 68,617 (151)

Histidine and Aspartic Acid Residues Important for Immunoglobulin G Endopeptidase Activity of the Group A Streptococcus Opsonophagocytosis-Inhibiting Mac Protein

Infection and Immunity, 2003
James Musser, Benfang Lei Lei
exaly   +2 more sources

Preliminary Investigation on the Ameliorative Role Exerted by D-Aspartic Acid in Counteracting Ethane Dimethane Sulfonate (EDS) Toxicity in the Rat Testis

Animals, 2021
Simple Summary For proper fertility, the production of good-quality spermatozoa is essential. Nowadays, many environmental pollutants affect the spermatogenetic process, at different levels.
M. Venditti, M. Romano, F. Aniello, S. Minucci   +3 more
semanticscholar   +1 more source

Safety evaluation of the food enzyme mucorpepsin from Rhizomucor miehei strain DSM 29547

EFSA Journal, 2022
The food enzyme mucorpepsin (EC 3.4.23.23) is produced with the non‐genetically modified Rhizomucor miehei strain DSM 29547 by Chr. Hansen. The food enzyme is free from viable cells of the production organism.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (EFSA CEP Panel), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Joaquim Maia, Natalia Kovalkovicova, Simone Lunardi, Yi Liu, Andrew Chesson   +22 more
doaj   +1 more source

Safety evaluation of the thermolabile form of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164

EFSA Journal, 2022
The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non‐genetically modified microorganism Rhizomucor miehei strain MMR 164.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Jaime Aguilera, Magdalena Andryskiewicz, Davide Arcella, Natália Kovalkovičová, Yi Liu, Joaquim Maia, Sandra Rainieri, Andrew Chesson   +26 more
doaj   +1 more source

Safety evaluation of the native and thermolabile forms of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164

EFSA Journal, 2022
The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non‐genetically modified microorganism Rhizomucor miehei strain MMR 164 by Takabio. The enzyme is chemically modified to produce a thermolabile form.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Jaime Aguilera, Magdalena Andryskiewicz, Davide Arcella, Natália Kovalkovičová, Yi Liu, Joaquim Maia, Sandra Rainieri, Andrew Chesson   +26 more
doaj   +1 more source

A Novel Legumain-Like Protease in Macrobrachium nipponense: Identification, Characterization, and Function Analysis in Ovary Maturation

Frontiers in Endocrinology, 2022
Legumain, also called aspartic endopeptidase (AEP), is a member of the cysteine protease family and is involved in various physiological processes. In this study, we analyzed the characteristics of a novel legumain-like (named Mn-Lel) in the female ...
Sufei Jiang, Yiwei Xiong, Wenyi Zhang, Junpeng Zhu, Dan Cheng, Yongsheng Gong, Yan Wu, Hui Qiao, Hui Qiao, Hongtuo Fu, Hongtuo Fu   +10 more
doaj   +1 more source

Comparative proteomic analysis of differentially expressed proteins in the urine of reservoir hosts of leptospirosis. [PDF]

PLoS ONE, 2011
Rattus norvegicus is a natural reservoir host for pathogenic species of Leptospira. Experimentally infected rats remain clinically normal, yet persistently excrete large numbers of leptospires from colonized renal tubules via urine, despite a specific ...
Jarlath E Nally, Avril M Monahan, Ian S Miller, Ruben Bonilla-Santiago, Puneet Souda, Julian P Whitelegge   +5 more
doaj   +1 more source

In ovo Feeding of L-Leucine Improves Antioxidative Capacity and Spleen Weight and Changes Amino Acid Concentrations in Broilers After Chronic Thermal Stress

Frontiers in Veterinary Science, 2022
L-Leucine (L-Leu) was demonstrated to confer thermotolerance by in ovo feeding in broiler chicks and chickens in our previous studies. However, the L-Leu-mediated roles in recovering from the detrimental effects of heat stress in broilers are still ...
Guofeng Han, Yangyang Cui, Dan Shen, Mingyang Li, Yu Ren, Takashi Bungo, Vishwajit S. Chowdhury, Yansen Li, Chunmei Li   +8 more
doaj   +1 more source

Cathepsin E (EC 3.4.23.34) — a review

Folia Histochemica et Cytobiologica, 2012
Cathepsin E belongs to the third class of enzymes — hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that
Anna Worowska, Marek Gacko, Michał Chlabicz, Radosław Łapiński   +3 more
doaj   +1 more source

Histidine and Aspartic Acid Residues Important for Immunoglobulin G Endopeptidase Activity of the Group AStreptococcusOpsonophagocytosis-Inhibiting Mac Protein [PDF]

Infection and Immunity, 2003
ABSTRACTThe secreted Mac protein made by serotype M1 group AStreptococcus(GAS) (designated Mac5005) inhibits opsonophagocytosis and killing of GAS by human polymorphonuclear neutrophils. This protein also has cysteine endopeptidase activity against human immunoglobulin G (IgG).
Benfang, Lei, Mengyao, Liu, Elishia G, Meyers, Heather M, Manning, Michael J, Nagiec, James M, Musser   +5 more
openaire   +2 more sources