Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The hitherto existing results of determinations of enzymatic activities in stool are presented in this review. The chymotrypsin activity is diminished in advanced exocrine pancreatic insufficiency. The faecal alpha-amylase activity has up to now no significance in the diagnosis of pancreatic diseases. Up to five amylolytic enzyme activities are detectable. The alkaline phosphatase is mostly of intestinal origin. Up to 4 enzyme bands can be exhibited with the disc electrophoresis in polyacrylamide gel. Lysozyme and N-Acetyl-beta-D-glycosaminidase can also be detected in stool.
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PMID:[Faecal enzyme diagnostic (author's transl)]. 9 52

Twelve antigens were detected in crude group C streptococcal extracellular concentrates, using naturally occurring antibodies in normal human gamma globulin. These group C streptococcal antigens all appeared to be present in crude group A streptococcal extracellular concentrates, although the latter contained additional antigens reactive with the human antibodies. Systematic purification procedures were established for the isolation of the group C streptococcal antigens by a sequence of salting out, hydroxylapatite chromatography, Sephadex G-100 gel filtration, and isoelectric focusing. With such procedures, three of the group C streptococcal antigens were isolated in a relatively pure state. One of the purified antigens was identified as streptokinase on the basis of its fibrinolytic potency, its reaction of identity with two purified streptokinase fractions obtained from other sources, and its high titer in immunodiffusion assays. The most highly purified streptokinase fractions, derived from the 0.1 M sodium phosphate hydroxylapatite eluate, revealed a plasmin-inhibiting effect at high concentrations of streptokinase. This was not seen in the purified streptokinase of equivalent functional and immunological purity that was derived from the 0.2 M sodium phosphate hydroxylapatite peak. Two other streptococcal antigens were also isolated to a high degree during the course of the above study. These were designated antigens X and Y and were found to be unrelated immunologically to each other or to streptokinase. Their isoelectric points were 6.7 and 8.8, respectively, and both were present in group A streptococcal concentrates. Esterase activity was found to be widely distributed in almost all of the fractions obtained in the various purification steps, indicating a high degree of heterogeneity of the streptococcal enzyme. Histochemical staining techniques applied to the immune precipitates formed with human antibodies indicated that none of the antigens detected in crude group C and group A streptococcal concentrates possessed catalase, glucuronidase, glucosaminidase, acid or alkaline phosphatase, arylsulfatase, leucineaminopeptidase, or chymotrypsin enzymatic activities.
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PMID:Purification of group C streptococcal extracellular antigens detected with naturally occurring human antibodies: isolation of streptokinase and two previously undescribed antigens. 13 Nov 8

The activity of the membrane-bound enzymes of the microvillous zone of the entreocytes (maltase, sucrase, trehalase, lactase, cellobiase, alkaline phosphatase and leucylaminopeptidase) was studied in mucosal smears from the proximal jejunum, ileum, caecum and sigmoid flexure in a group of control (C) (8) and germ-free (GF) (7) rabbits. The trypsin and chymotrypsin activity of the contents of the ileum, caecum and sigmoid flexure was studied in 6 C, 5 GF and 5 monocontaminated (MC) rabbits. In summing up it can be stated that the individual membrane-bound enzymes have a different gradient in the various intestinal segments of C and GF rabbits and that they differ reciprocally in character. The maximum statistically significant differences between GF and C rabbits were found in the ileum; in the jejunum they were somewhat smaller and in the caecum smaller still (in this localization the difference was C versus GF). Striking differences in the proportion of the individual disaccharidases were found inthe jejunum and ileum of C rabbits compared with GF rabbits, in which, in both these segments of small intestine the relationship maltase greater than sucrase greater than trehalase greater than lactase was preserved. The proteolytic activity of the intestinal contents likewise had a different gradient character in C, MC and GF rabbits. The maximum activities (especially trypsin) were found in MC animals. The microbial flora is one of the factors regulating the enzymatic activities of the microvillous zone of the enterocytes and it also significantly influences the proteolytic activity of the intestinal contents. This influence is particularly marked in the distal part of the alimentary tube.
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PMID:Digestive enzymes of the mucosa of the small intestine and trypsin and chymotrypsin proteolytic activity of the intestinal contents of germ-free, monocontaminated and conventional rabbits. 35 55

Bacterial extracts were prepared from cultures originating in chronic self-filling intestinal blind loops in rats. Their ability to remove active maltase molecules from isolated brush border membranes was studied in vitro. Twelve strains in 51 tested, belonging to one of three species, Bacteroides fragilis, Clostridium perfringens, and Streptococcus fecalis, possessed maltase-releasing activity. The ability to remove maltase correlated well with the ability to hydrolyze p-nitrophenyl-tert-butyloxycarbonyl-l-alaninate (NBA), an ester substrate rapidly hydrolyzed by elastase, but not with substrated favored by tryhsin and chymotrypsin. Maltase-releasing activity from C. perfringens was strongly inhibited by soybean trypsin inhibitor and to a lesser extent by lima bean trypsin inhibitor. Of four chloromethylketone active-site directed inhibitors tested with specificities for elastase, trypsin, and chymotrypsin, inhibition was maximal with elastase-specific inhibitors. In two species, activity was shown to be heat sensitive, and to be inhibited by concentration of the extract. In one species maltase-releasing activity was shown to be due to an enzyme of molecular weight at least 66,000 with the capacity to remove lactase, sucrase, and alkaline phosphatase, as well as maltase. The results indicate that anaerobic or facultatively anaerobic species, previously identified with the pathology of of the blind loop syndrome, contain proteases which are capable of removing components of the intestinal surface membrane. These proteases appear to have elastase-like substrate specificity and may be involved in the etiology of disaccharidase deficiency in bacterial overgrowth syndromes.
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PMID:Pathogenesis of mucosal injury in the blind loop syndrome. 35

At 20 degrees C, aflatoxin B1, at a sublethal dose, decreases the activity of alkaline phosphatase (EC 3.1.3.1), alpha-glucosidase (EC 3.2.1.20), esterase (EC 3.1.1.1), chymotrypsin (EC 3.4.21.1), leucine aminopeptidase (EC 3.4.11.1), and phosphoamidase (EC 3.9.1.1) biosynthesis in Bacillus thuringiensis (Berliner). In contrast, at 41 degrees C no significant decrease was observed. At this temperature, the mycotoxin is not destroyed or metabolized and bacterial cells are resistant to the toxin.
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PMID:[Effect of aflatoxin B1 on the enzymatic activities of Bacillus thuringiensis (Berliner)]. 88 28

Nuclear magnetic quadrupole relaxation appears to be a general method for studying the binding of anions to proteins. This is shown by the increase in transverse quadrupole relaxation rate of 35Cl- and 81Br- in the presence of horse liver alcohol dehydrogenase, lysozyme, trypsin, alpha-chymotrypsin, human carbonic anhydrase, fructose-1,6-bisphosphate aldolase and human serum albumin. Of the many possible binding sites at the surface of a protein (e.g. positively charged amino acid side-chains) only a few account for the main part of the relaxation enhancement. This is shown by the decrease in 35Cl- and 81Br- relaxation rate on addition of functional ligands. Large, kinetically inert, complex anions like Pt(CN)2-4 and Au(CN)-2 are found to act as strong competitors towards halogen ions for the high-affinity anion binding sites of a number of proteins. Titrations with complex anions following the 35Cl- or 81Br- relaxation rates are found to be helpful in attempts to elucidate binding mechanisms. Especially, the complex anions may be useful probes for the discrimination between general and metallic anion binding sites in proteins and they also permit correlation of information from X-ray investigations of crystals with that from physical measurements in solution. From the change in halide ion quadrupole relaxation rate on addition of strongly binding ligands the quadrupole coupling constants of the high affinity Cl- and Br- binding sites are estimated using certain assumptions. It is found that for several proteins, comprising the metal-free proteins but also alcohol dehydrogenase and Escherichia coli alkaline phosphatase, the 35Cl quadrupole coupling constants have approximately the same values. For some other metallo-proteins like carbonic anhydrase and a zinc - serum-albumin complex considerably greater quadrupole coupling constants were obtained. The estimated quadrupole coupling constants are used as a basis for a discussion of the interactions involved in anion-protein interactions.
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PMID:Pt(CN)2-4 and Au(CN)-2: potential general probes for anion-binding sites of proteins. 35Cl and 81Br nuclear-magnetic-resonance studies. 120 23

The releases of proteins, maltase, lactase, sucrase, trehalase, alkaline phosphatase, gamma-glutamyltransferase and leucylnaphthylamide-hydrolyzing activity from human intestinal brush bborder membrane vesicles by various enzymes (especially pancreatic proteases) have been studied. The brush border membrane enzymes are not solubilized by digestion with trypsin and chymotrypsin but are largely released after treatment with papain or elastase. Most of the enzymes are fully active after the proteolytic treatment. All proteins released by papain and elastase have been identified by electrophoresis to already known intestinal hydrolases. Electron microscopy of brush border membrane vesicles demonstrates "knob-like" structures (particles) attached to the external side of the membrane. During papain treatment, enzyme removal runs parallel with the disappearance of the particles. During elastase treatment it is not possible to correlate the release of the enzymic activities with the removal of the particles. The results indicate that most of the intestinal hydrolases are surface components attached to the external side of the membrane. They are in accord with the concept that the brush border membrane enzymes are organized within the membrane in a mosaic-like pattern.
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PMID:Enzymic solubilization of the human intestinal brush border membrane enzymes. 127 90

Sertoli cell intracellular protein 1 (SCc1) and 2 (SCc2) are polypeptides found in rat Sertoli cell cultures incubated with either FSH or (Bu)2cAMP. They were first identified in [35S]methionine-labeled Sertoli cell lysates using two-dimensional gel electrophoresis. Here we extend these observations by showing that SCc1 and SCc2 are present in rat seminiferous tubules, ovaries, and granulosa cells incubated with either FSH or (Bu)2cAMP and in testicular peritubular cells incubated with (Bu)2cAMP. Peritubular cells do not, however, respond to FSH with the production of SCc1 and SCc2. Peptide mapping with N-chlorosuccinimide revealed that SCc1 and SCc2 have similar cleavage patterns, suggesting a common primary amino acid sequence that is modified posttranslationally. Metabolic labeling with [32P]orthophosphate provided direct evidence that SCc1 and SCc2 are phosphoproteins. A shift in mobility of SCc1 and SCc2 toward the basic region of the gel to positions designated SCc1' and SCc2' occurred when cell lysates were treated with alkaline phosphatase before electrophoresis, providing additional evidence that SCc1 and SCc2 are phosphoproteins. SCc1 and SCc2 are also shown to be mitochondrially-associated in the Sertoli cell. Peptide maps of SCc1, SCc2, SCc1', and SCc2' obtained by treatment with alpha-chymotrypsin, are identical to proteolytic maps of proteins pp30', p30, and pp30 from adrenocortical cells. SCc1, SCc2, SCc1', and SCc2' are homologous with regard to their regulated expression, electrophoretic mobility, and mitochondrial localization to the adrenal proteins pp30' and pp30 as well as a series of 30 kilodalton proteins from MA-10 Leydig tumor cells. Both the adrenal cell proteins and the Leydig tumor cell proteins are thought to participate in cholesterol transport to the inner mitochondrial membrane, providing substrate for the cholesterol side-chain cleavage enzyme complex, an activity which the Sertoli cell does not perform, suggesting that alternative functions must be sought for SCc1 and SCc2 in Sertoli cells.
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PMID:Follicle-stimulating hormone-regulated Sertoli cell proteins SCc1 and SCc2 are phosphorylated and mitochondrially associated. 133 Apr 90

The purpose of this study was to assess the relationship of neuropeptide nerves and inflammatory leukocytes in PVG rats with adjuvant-induced arthritis. Substance P- and calcitonin gene-related peptide (CGRP)-immunoreactive nerves and inflammatory leukocytes were studied, using peroxidase (ABC) and/or alkaline phosphatase (APAAP) staining. Inflamed synovial tissue proper was infiltrated with neutrophils, ED1 macrophages and focal accumulations of CD2 T lymphocytes. In such tissue, the relationship between peptide-immunoreactive nerves and inflammatory cells was such that substance P and CGRP nerves were absent in heavily infiltrated villous synovial tissue, whereas healthy synovial tissue and non-inflammatory areas in adjuvant arthritic rats were innervated by substance P and CGRP nerves close to normal synovial tissue resident cells. In order to elucidate an eventual mechanism for lost immunoreactivity, healthy synovial tissue was exposed to chymotrypsin or oxygen derived free radicals (ODFR) in vitro. The former treatment caused total loss of immunoreactivity. These findings suggest that neuropeptides and neuropeptide containing nerves may be destroyed by locally produced proteolytic enzymes and various reactive oxygen species in the vicinity of inflammatory cells.
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PMID:Relationship between neuropeptide immunoreactive nerves and inflammatory cells in adjuvant arthritic rats. 137 4

A simple convenient method has been developed for the quantitation of serine proteinase inhibitors (SPIs) in tissue extracts. The method is based on the competitive binding to trypsin and chymotrypsin immobilized using glutaraldehyde on 96-well microtiter plate wells of native SPIs and a biotinylated secretory proteinase inhibitor (SLPI) standard. The bound SLPI standard was visualized using an avidin-alkaline phosphatase conjugate and inhibition curves were determined using absorbancy measurements at 405 nm. The standard assay had a range between 0.02 and 1 microgram SLPI/well and a lower detection limit of 20 ng SLPI/well; an improved microassay had a detection limit of 2 ng SLPI/well. Only active free inhibitor was detected in the assay since denatured and/or enzyme-inhibitor complexes did not bind to the plates. A range of SPI species was demonstrable in human bronchial mucus and intervertebral disc SPI samples using this technique. Quantitation of SPI levels in a number of intervertebral disc samples indicated that the SPIs were depleted in degenerate discs compared to nondegenerate discs (P less than 0.05, n = 12). Since the immobilized trypsin and chymotrypsin microplates used in this assay may be prepared in advance (and are stable at 4 degrees C for at least 1 month) the remaining two steps of the assay (the inhibition step and visualization) may be completed in 2-3 h; thus the assay is simple, convenient, and fast. All reagents (other than the biotinylated SLPI standard) are readily available commercially, and in principle the assay could be adapted to other systems provided defined biotinylated standards were available.
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PMID:Development of an avidin-biotin competitive inhibition assay and validation of its use for the quantitation of human intervertebral disc serine proteinase inhibitory proteins. 144 38


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