Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two electrophoretic vari ants of leucine aminopeptidase show direct association with two genetically controlled forms of alkaline phosphatase. Treatment of plasma with neuraminidase converted the faster-migrating form of both enzymes to slower-moving forms, but plasmas with slowermigrating forms were unaffected by this treatment. The two forms of the enzymes may be due to the presence or absence of a single gene controlling the attachment of sialic acid to the enzyme molecules.
 ...
PMID:Alkaline phosphatase and leucine aminopeptidase association in plasma of the chicken. 602 89

The three brush-border enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), and gamma-glutamyltransferase (EC 2.3.2.2)--are present in the urine of healthy persons in two variants, a particulate form and a soluble one. They can be separated by electrophoresis in agarose gel and by ultracentrifugation. The particulate forms exhibit similar electrophoretic mobility, but the soluble forms of these brush-border enzymes differ in their electrophoretic mobilities. The enzyme components of the particulate activity can be mobilized by Triton X-100 and trypsin. The electrophoretic mobility of the soluble forms of alanine aminopeptidase and gamma-glutamyltransferase is slowed by neuraminidase treatment. Both forms of gamma-glutamyltransferase are influenced in their electrophoretic mobility by treatment with n-butanol/diisopropyl ether, showing their lipid dependence. These findings enhance our knowledge of the biochemical nature of brush-border enzymes in urine.
 ...
PMID:Electrophoretic variants of alanine aminopeptidase, alkaline phosphatase, and gamma-glutamyltransferase in urine. 614 5

Cerebroside sulfatase also known as arylsulfatase A from human liver displays six microheteromer bands upon narrow pH range isoelectric focusing. Sialic acid residues only partially account for this enzyme multiplicity since neuraminidase treatment reduces the number of bands to three. Uptake studies with cultured fibroblasts strongly suggest arylsulfatase A has covalently bound mannose 6-phosphate residues. However, treatment with alkaline phosphatase and a battery of glycohydrolases failed to reduce the number of enzyme charge forms below three. These results imply that the neuraminidase-resistant charge microheterogeneity is not due to structures associated with the carbohydrate moiety of arylsulfatase A.
 ...
PMID:Microheterogeneity of arylsulfatase a: Treatment with hydrolytic enzymes. 614 17

Purpura was grossly observable in albino mice 6 to 8 h after the intraperitoneal injection of sterile, deoxyribonuclease-treated, cell-free extracts prepared by sodium deoxycholate-induced lysis, sonic disruption, Parr bomb treatment, autolysis without sodium deoxycholate, or alternate freezing and thawing of washed suspensions of Streptococcus pneumoniae type I. Cell-free extracts obtained from sonically disrupted, heat-killed cells (100 degrees C for 20 min) did not contain purpurogenic activity. The reaction was maximal at approximately 24 h postinjection, started to fade slowly after 24 to 48 h, and usually was not grossly observable by 4 to 6 days postinjection. The purpura-producing principle (PPP) in the cell-free extract was purified by sequential ammonium sulfate precipitation, protamine sulfate precipitation, Sepharose 6B gel filtration, wheat germ lectin-Sepharose 6MB affinity chromatography, ribonuclease and trypsin treatment, and a second Sepharose 6B gel filtration step. The final preparation (i) contained glucosamine (5.6%), muramic acid (8.0%), neutral carbohydrate (12.8%), phosphate (8.0%), orcinol-reactive material (6.0%), and Lowry-reactive material (1.6%), and (ii) was free of detectable amounts of deoxyribonucleic acid, capsular polysaccharide, neuraminidase, cytolysin, and hyaluronidase. The isoelectric point and molecular size of the PPP were approximately pI 3.0 and several million daltons, respectively, and the activity remained in the supernatant fluid after centrifugation for 1 day at 105,000 x g. PPP activity was destroyed by incubation with egg white lysozyme and sodium metaperiodate but was resistant to trypsin, pronase, alpha-amylase, deoxyribonuclease, ribonuclease, alkaline phosphatase, pancreatic lipase, 7% trichloroacetic acid, 6 M urea, autoclaving (121 degrees C) for 30 min, and mild acid and alkali exposure. Our observations indicate that the PPP requires intact beta-1,4-glucosidic linkages for activity and support the working hypothesis that activity is associated with pneumococcal peptidoglycan solubilized by the bacterium's autolysin.
 ...
PMID:Characterization of pneumococcal purpura-producing principle. 624 53

Two enzyme forms of alkaline phosphatase have been partially purified from the medium spent for the culture of HUH-6 clone 5 cells, which were originally derived from hepatoblastoma tissue. The purification methods used are ammonium sulfate precipitation, ethanol precipitation, diethylaminoethyl cellulose chromatography, Affi-Gel Blue chromatography, and Sephadex G-200 gel filtration. These alkaline phosphatases have been characterized by thermostability, inhibition, and immunological and electrophoretic studies. Both are L-phenylalanine and L-tryptophan sensitive and L-homoarginine and L-leucylglycylglycine insensitive, and both react with an antiserum against intestinal alkaline phosphatase. The major enzyme form is a neuraminidase-cleavable, moderately thermostable isoenzyme which on polyacrylamide gel shows an electrophoretic mobility similar to that of liver alkaline phosphatase. The minor enzyme form is a neuraminidase-uncleavable, thermolabile isoenzyme which shows an intermediate electrophoretic mobility between liver and hepatoma alkaline phosphatases. The molecular weights of the major and minor enzymes have been estimated by gel filtration to be 170,000 and 110,000, respectively. These results support the conclusion that the two enzyme forms of HUH-6 alkaline phosphatase are intestinal in type, with the major enzyme form closely resembling hepatoma and oncoamnionic alkaline phosphatases, and the minor enzyme form resembling "intestine-like liver alkaline phosphatase." HUH-6 clone 5 cell line may be a useful in vitro model to study the regulatory mechanism for phenotypic expression of intestinal-type alkaline phosphatase isoenzymes in liver cancer cells.
 ...
PMID:Intestinal-type alkaline phosphatase produced by human hepatoblastoma cell line HUH-6 clone 5. 631 71

An enzymatic radioimmunoassay for influenza A virus was developed by using polystyrene beads coated with rabbit immunoglobulin G to capture viral hemagglutinins (H1 and H3). Captured hemagglutinin was detected with goat immunoglobulin G followed by affinity-purified rabbit anti-goat immunoglobulin G labeled with alkaline phosphatase. [3H]AMP was added to quantify alkaline phosphatase activity, and free [3H]adenosine was measured with a scintillation counter. The assay detected as little as 0.1 ng of purified hemagglutinin. It was specific for hemagglutinin subtype and, depending on the source of the goat immunoglobulin G used, detected either H1 or H3. There was no reaction with neuraminidase or core antigens of influenza strain WSN-33. The clinical efficacy of the assay was evaluated with sequential nasal washes from 33 patients with naturally acquired H1N1 influenza. In the first 3 days of infection, the assay was consistently less sensitive than the viral culture, although detectable antigen persisted in secretions longer than did the infectious virus. Testing of multiple samples greatly increased the number of individuals in whom an etiological diagnosis could be made by immunoassay (81% of patients were positive for viral antigens at some point in their illness), and such testing was necessary to achieve the sensitivity of a single culture. Mean antigen levels were highest in nasal washes with the highest titers of infectious virus.
 ...
PMID:Etiological diagnosis of influenza A virus by enzymatic radioimmunoassay. 637 Oct 41

Alkaline phosphatase from human uterine myoma was purified to homogeneity by butanol extraction, acetone precipitation, column chromatography on DEAE-cellulose, QAE-Sephadex and Con-A-Sepharose, gel filtration on Sephadex G-200 and preparative electrophoresis. The relative molecular mass (145 000), subunit mass (35 000), neutral sugars (7 micrograms/mg) and sialic acid (1 microgram/mg) content were estimated. pH optimum of the enzyme activity was 10.0-10.4, and Km for p-nitrophenyl phosphate was 0.23 mM. The enzyme was inhibited by Zn2+, phosphate, fluoride, EDTA and by treatment with neuraminidase. Mg2+ activated alkaline phosphatase and showed protective effect towards inhibition by EDTA and Zn2+. The uterine muscle alkaline phosphatase was also purified. It showed lower specific activity than myoma phosphatase, higher molecular mass (160 000) and subunit mass (76 400), higher neutral sugar and sialic acid content.
 ...
PMID:Alkaline phosphatase from human uterine myoma. I. Purification and some properties. 642 57

Mouse ileal alkaline phosphatase is a sialyl enzyme (12-14 moles per mole of enzyme). When partially desialylated by treatment with neuraminidase, the enzyme loses most of its activity, associated with reduced apparent Vmax and Km. Part of that loss, however, is recovered as the product 4-nitrophenol's concentration builds up in the cuvette. Experimental results are presented to demonstrate that the activation is due to the binding of 4-nitrophenol as a ligand by the partially desialylated enzyme and that both the loss of activity by sialic acid removal and activation by ligand-binding are correlated with changes in protein conformation.
 ...
PMID:Desialylated alkaline phosphatase: activation by 4-nitrophenol. 647 97

The adult and fetal forms of human intestinal alkaline phosphatase (ALPase; orthophosphoric-monoester phosphohydrolase, EC 3.1.3.1) are indistinguishable by a variety of analytical procedures. However, they differ electrophoretically and can be differentiated by binding studies with monoclonal antibodies. In this report, these two enzymes along with placental and liver ALPases are compared by the technique of CNBr peptide mapping, and the role of carbohydrate in generating these patterns is investigated. NaDodSO4/PAGE of CNBr digests of radiolabeled ALPases from fetal and adult intestine shows that these two isozymes share five of seven common-sized CNBr fragments. Placental ALPase shares only one common-sized fragment with either intestinal enzyme. Liver ALPase has no CNBr fragments in common with any of the others. These data indicate that fetal intestinal ALPase is not a heterodimer of one subunit each of intestinal ALPase and placental ALPase as has been postulated. CNBr digests of neuraminidase-treated enzymes reveal a change of mobility of only one CNBr band in each of fetal intestinal, placental, and liver ALPases, indicating the presence of sialic acid residues in these fragments. Periodic acid/Schiff reagent staining (specific for carbohydrate) of CNBr digests of fetal and adult intestinal ALPases reacts with only one band in each enzyme, which is the same band from the fetal enzyme shown to contain sialic acid. However, fetal and adult intestinal ALPases each contain at least one CNBr fragment of unique size that is apparently nonglycosylated.
 ...
PMID:Structural analysis of human adult and fetal alkaline phosphatases by cyanogen bromide peptide mapping. 659 4

Four inbred strains of mice exhibited either slow (PL/J), intermediate (DBA/2J, LP/J), or fast (SWR/J) rates of migration of duodenal alkaline phosphatase on cellulose acetate electrophoresis. Hybrids of these strains also had intermediate rates of migration regardless of the combination of strains used as parents. Strain differences were present in all regions of the small but not the large intestine. Crosses of the PL/J strain to hybrids between this strain and the other three strains gave a 1:1 segregation of the slow and intermediate patterns. The symbol Akp-3 is proposed for the locus responsible for the slower migration of the enzyme in this strain. Data from the LP/J X PL/J hybrid crossed with the PL/J strain showed linkage with two loci on chromosome 1 as follows: centromere--Idh-1--13.8 cM--Akp-3--8.9 +/- 2.6 cM--Pep-3. The available data do not reveal the genetic basis for the faster migration rate of the enzyme from the SWR/J strain, but a different response to neuraminidase and apparent nonlinkage to the Pep-3 locus suggest that a locus other than Akp-3 is responsible.
 ...
PMID:Genetics of alkaline phosphatase of the small intestine of the house mouser (Mus musculus). 662 38


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>