| D007527 |
Isoenzymes |
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. |
Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes |
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| D007931 |
Leucyl Aminopeptidase |
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. |
Cytosol Aminopeptidase,Leucine Aminopeptidase,L-Leucylnaphthylamidase,Methoxyleucine Aminopeptidase,Peptidase S,Zinc-Manganese-Leucine Aminopeptidase,Aminopeptidase, Cytosol,Aminopeptidase, Leucine,Aminopeptidase, Leucyl,Aminopeptidase, Methoxyleucine,Aminopeptidase, Zinc-Manganese-Leucine,Zinc Manganese Leucine Aminopeptidase |
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| D008667 |
Metalloproteins |
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) |
Metalloprotein |
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| D011247 |
Pregnancy |
The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH. |
Gestation,Pregnancies |
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| D011270 |
Pregnancy, Animal |
The process of bearing developing young (EMBRYOS or FETUSES) in utero in non-human mammals, beginning from FERTILIZATION to BIRTH. |
Animal Pregnancies,Animal Pregnancy,Pregnancies, Animal |
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| D001826 |
Body Fluids |
Liquid components of living organisms. |
Body Fluid,Fluid, Body,Fluids, Body |
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| D004971 |
Estrus |
The period in the ESTROUS CYCLE associated with maximum sexual receptivity and fertility in non-primate female mammals. |
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| D005260 |
Female |
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Females |
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| D000071681 |
Tartrate-Resistant Acid Phosphatase |
One of several acid phosphatases in humans, other mammals, plants, and a few prokaryotes. The protein fold of tartrate-resistant acid phosphatase (TRAP) resembles that of the catalytic domain of plant purple acid phosphatase and other serine/threonine-protein phosphatases that also contain a metallophosphoesterase domain. One gene produces the various forms which include purple acid phosphatases from spleen and other tissues. Tartrate-resistant acid phosphatase is a biomarker for pathological states in which it is over-expressed. Such conditions include GAUCHER DISEASE; HODGKIN DISEASE; BONE RESORPTION; and NEOPLASM METASTASIS. |
AcPase V,Acid Phosphatase V,TRAP Type 5 AcPase,TRAcP,Tartrate-Resistant Acid Phosphatase Type 5,Type 5 Acid Phosphatase,Uteroferrin,Acid Phosphatase, Tartrate-Resistant,Phosphatase V, Acid,Phosphatase, Tartrate-Resistant Acid,Tartrate Resistant Acid Phosphatase,Tartrate Resistant Acid Phosphatase Type 5,V, AcPase,V, Acid Phosphatase |
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| D000135 |
Acid Phosphatase |
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2. |
Acid beta-Glycerophosphatase,Acid beta Glycerophosphatase |
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