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76768 Ensembl ENSG00000163283 ENSMUSG00000079440 UniProt P05187 F8VPQ6 RefSeq (mRNA) NM_001632 NM_001081082 RefSeq (protein) NP_001623 NP_001074551 Location (UCSC) Chr 2: 232.38 – 232.38 Mb Chr 1: 87.03 – 87.03 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Alkaline phosphatase, placental type also known as placental alkaline phosphatase (PLAP) is an allosteric enzyme that in ...
Liver function tests (LFTs or LFs), also referred to as a hepatic panel or liver panel, are groups of blood tests that provide information about the state of a patient's liver. [1] These tests include prothrombin time (PT/INR), activated partial thromboplastin time (aPTT), albumin , bilirubin (direct and indirect), and others.
The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic ...
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]
Aspartoacylase is a hydrolytic enzyme (EC 3.5.1.15, also called aminoacylase II, ASPA and other names [a]) that in humans is encoded by the ASPA gene.ASPA catalyzes the deacylation of N-acetyl-l-aspartate (N-acetylaspartate) into aspartate and acetate.
Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [ 13 ] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation ...
The systematic name of this enzyme class is 2-methylacyl-CoA 2-epimerase. In vitro experiments with the human enzyme AMACR 1A show that both (2S)- and (2R)-methyldecanoyl-CoA esters are substrates and are converted by the enzyme with very similar efficiency. Prolonged incubation of either substrate with the enzyme establishes an equilibrium ...