| D007700 |
Kinetics |
The rate dynamics in chemical or physical systems. |
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| D010450 |
Endopeptidases |
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. |
Endopeptidase,Peptide Peptidohydrolases |
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| D010740 |
Phospholipases |
A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-. |
Lecithinases,Lecithinase,Phospholipase |
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| D002175 |
Candida |
A genus of yeast-like mitosporic Saccharomycetales fungi characterized by producing yeast cells, mycelia, pseudomycelia, and blastophores. It is commonly part of the normal flora of the skin, mouth, intestinal tract, and vagina, but can cause a variety of infections, including CANDIDIASIS; ONYCHOMYCOSIS; VULVOVAGINAL CANDIDIASIS; and CANDIDIASIS, ORAL (THRUSH). |
Candida guilliermondii var. nitratophila,Candida utilis,Cyberlindnera jadinii,Hansenula jadinii,Lindnera jadinii,Monilia,Pichia jadinii,Saccharomyces jadinii,Torula utilis,Torulopsis utilis,Monilias |
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| D002176 |
Candida albicans |
A unicellular budding fungus which is the principal pathogenic species causing CANDIDIASIS (moniliasis). |
Candida albicans var. stellatoidea,Candida stellatoidea,Dematium albicans,Monilia albicans,Myceloblastanon albicans,Mycotorula albicans,Parasaccharomyces albicans,Procandida albicans,Procandida stellatoidea,Saccharomyces albicans,Syringospora albicans |
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| D002177 |
Candidiasis |
Infection with a fungus of the genus CANDIDA. It is usually a superficial infection of the moist areas of the body and is generally caused by CANDIDA ALBICANS. (Dorland, 27th ed) |
Candida Infection,Moniliasis,Candida Infections,Candidiases,Infection, Candida,Moniliases |
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| D002808 |
Chondroitin Lyases |
Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C. |
Chondroitin AC Lyase,Chondroitin B Lyase,Chondroitin Eliminase,Chondroitin Sulfate Lyase,Chondroitinase-AC II,Chondroitinase AC II,Eliminase, Chondroitin,Lyase, Chondroitin AC,Lyase, Chondroitin B,Lyase, Chondroitin Sulfate,Lyases, Chondroitin,Sulfate Lyase, Chondroitin |
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| D006821 |
Hyaluronoglucosaminidase |
An enzyme that catalyzes the random hydrolysis of 1,4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. (From Enzyme Nomenclature, 1992) There has been use as ANTINEOPLASTIC AGENTS to limit NEOPLASM METASTASIS. |
Hyaluronidase,Duran-Reynals Permeability Factor,GL Enzyme,Hyaglosidase,Hyaluronate Hydrolase,Wydase,Duran Reynals Permeability Factor,Factor, Duran-Reynals Permeability,Hydrolase, Hyaluronate,Permeability Factor, Duran-Reynals |
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| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
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| D013045 |
Species Specificity |
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species. |
Species Specificities,Specificities, Species,Specificity, Species |
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