Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eschscholtzia californica stigmas with germinating pollen at different stages of development were the subject of histochemical studies which aimed the localization of several enzymes like phosphorylase, leucine amino peptidase, nonspecific esterase, cytochrome oxidase, aldolase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, monoamine oxidase, alpha-galactosidase, beta-glucosidase and beta-galactosidase. Pollen and pollen tubes were shown to contain starch, lipid, proteins and soluble sugars as the storage products. These storage products were utilized during germination and tube growth. The role of different enzymes in the process of germination and tube growth is discussed. From the distribution of oxidoreductases it is inferred that respiration plays an essential role in the tube growth. During pollen germination probably the reserve proteins were transported to pollen tube tip. The increase of activity of alpha-and beta-galactosidase in pollen tubes indicates on their involvement in carbohydrate metabolism. The role of alpha-galactosidase in the metabolism of galactolipids is also inferred. Similarly, the reaction catalysed by beta-glucosidase resulted in the production of aglycon and glucose; of these the former possibly act as a substrate of peroxidase. Some of the glycosidases diffused out of pollen wall on the stigma and participated in the release of free sugars of the female tissue.
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PMID:Studies on the physiology of pollen and pollen tube growth. IV Eschscholtzia californica Cham. 22 Jan 58

Several classes of proteolytic enzymes were used to gain an insight into the biochemical composition of the antiotensin II (ATII) receptor prepared from bovine adrenal cortices. Exposure of the receptor fractions to trypsin reduced their capacity to bind [3H]ATII. Phospholipases A2 and C similarly inhibited the [3H]ATII binding process, while phospholipase D had no effect. Binding was stimulated following addition of phosphatidylcholine but inhibited by lysophosphatidylcholine. Neuraminidase had no influence on [3H]ATII affinity for binding, while beta-galactosidase reduced binding of the radioligand. Concanavalin A did not displace [3H]ATII bound to receptor fractions. Very little aminopeptidase activity was detected in the receptor fraction, relative to the homogenate. The data suggest that the ATII recognition sites contain protein moieties, while phospholipids may play an essential role in ATII binding. Galactose units may form a part of the ATII receptor not directly associated with the binding site. The peptidase studies indicate that ATII probably cannot be hydrolyzed to its des-Asp1 metabolite at or near the site of binding.
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PMID:Enzymatic modifications of bovine adrenocortical angiotensin II receptors. 22 26

A brush-border-specific antiserum was raised in rabbits, with Triton X-100-solubilized brush border proteins from pig intestine being used as antigens. The antiserum was used in immunoelectrophoretic studies of brush border proteins solubilized with Triton X-100. Five immunoprecipitates were obtained which corresponded to microsomal aminopeptidase (EC 3.4.11.2), asparate aminopeptidase (EC 3.4.11.7), lactase (beta-galactosidase, EC 3.2.1.23), maltase (exo-1,4-alpha-glucosidase, EC 3.2.1.3) and sucrase-isomaltase (sucrose alpha-glucohydrolase, EC 3.2.1.48). A faint immunoprecipitate was also found for the glycylprolyl dipeptidyl peptidase (EC 3.4.14.-). The brush border proteins were solubilized on a large scale from a brush border membrane preparation by the use of Triton X-100; the peptidases obtained were homogeneous in size and had hydrophobic properties. By chromatography on columns of concanavalin A-Sepharose, hydroxyapatite, Ultrogel AcA 34, DEAE-cellulose and immunosorbent, gamma-glutamyl transpeptidase (gamma-glutamyl transferase, EC 2.3.2.2) and microsomal aminopeptidase were each isolated in separate fractions. Glycylprolyl dipeptidyl peptidase and asparate aminopeptidase were obtained in another fraction. Immunoelectrophoretic, inhibitor and chromatographic studies showed that the intestinal brush border peptidases are similar to the corresponding particulate peptidases obtained from other organs.
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PMID:Intestinal brush border peptidases. 24 83

Urinary dilution adjustment methods can be used to reduce the intra-individual variability in concentrations of metals and other substances in urine due to variability in urinary flow. In this study linear and non-linear dilution adjustments with urinary flow, creatinine (CREAT) and urinary density (UD) were compared for the urinary enzymes alanine amino peptidase (AAP), beta-galactosidase (beta GAL) and N-acetyl-beta, D-glucosaminidase (NAG). The most optimal dilution adjustment for AAP was: AAPadjusted = AAPmeasured/(CREATmeasured)0.824 The optimal dilution adjustment for beta GAL was: beta GALadjusted = beta GALmeasured/(CREATmeasured)0.878 For NAG the optimal dilution adjustment parameter was the conventional linear adjustment with SG. It could not be determined whether urinary dilution methods can be useful for population based reference intervals of urinary enzymes. If personal reference intervals can be calculated, urinary dilution adjustment methods may be useful by reduction of intraindividual variability.
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PMID:A comparison of dilution adjustment methods for urinary enzymes. 135 36

The main objective of the study was to investigate the effect of the calcium antagonists Verapamil (2 mg.kg-1.day) and Nifedipine (1 mg.kg-1.day-1) on cholesterol (1%) induced atherosclerosis in rabbits. The drugs were administered s.c. twice daily over a period of 8 weeks. Blood lipid levels were determined three times during the experiment. After the experimental period the animals were killed and macroscopic changes on the aorta were recorded. For histochemical investigation samples were taken from the arch of the aorta and coronary artery. In cryostat sections lipids were determined by Sudan black B and Fett rot 7 B and the following enzymes were assayed: acid phosphatase, non-specific and acid esterase, acid beta-galactosidase, dipeptidyl peptidase I and II, and glucose-6-phosphate dehydrogenase. Following treatment with the calcium antagonists the levels of triacylglycerols and of total cholesterol were significantly increased in comparison with the control and diet groups. The ratio of HDL cholesterol to total cholesterol decreased in the treated animals. In lipoid plaques the activity of enzymes was enhanced in all experimental animals. There were however no qualitative differences in the composition of plaques between individual groups, which exhibited only quantitative differences. The number of migrating macrophages was increased only in the nifedipine treated animals. The extent of plaques was significantly decreased after nifedipine treatment, whereas verapamil failed to exert antiatherogenic effect. (Tab. 2, Fig. 4, Ref. 22.).
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PMID:[The effect of verapamil and nifedipine on the development of experimental atherosclerosis in rabbits]. 152 79

We discovered an enzyme in human platelets that deamidates substance P and other tachykinins. Because an amidated carboxyl terminus is important for biological activity, we purified and characterized this deamidase. The enzyme, released from human platelets by thrombin, was purified to homogeneity by ammonium sulfate precipitation, followed by chromatography on an octyl-Sepharose column and chromatofocusing on PBE 94. The purified enzyme exhibits esterase, peptidase, and deamidase activities. The peptidase activity (with furylacryloyl-Phe-Phe) is optimal at pH 5.0 while the esterase (benzoyl-tyrosine ethyl ester) and deamidase (D-Ala2-Leu5-enkephalinamide) activities are optimal at pH 7.0. With biologically important peptides, the enzyme acts both as a deamidase (substance P, neurokinin A, and eledoisin) and a carboxy-peptidase (with bradykinin, angiotensin I, substance P-free acid, oxytocin-free acid) at neutrality, although the carboxypeptidase action is faster at pH 5.5. Enkephalins, released upon deamidation of enkephalinamides, were not cleaved. Gly9-NH2 of oxytocin was released without deamidation. Peptides with a penultimate Arg residue were not hydrolyzed. Some properties of the deamidase are similar to those reported for cathepsin A. The deamidase is inhibited by diisopropylfluorophosphate, inhibitors of chymotrypsin-type enzymes, and mercury compounds while other inhibitors of catheptic enzymes, trypsin-like enzymes, and metalloproteases were ineffective. In gel filtration, the native enzyme has an Mr = 94,000 while in non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis the Mr = 52,000 indicating it exists as a dimer. After reduction, deamidase dissociates into two chains of Mr = 33,000 and 21,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. [3H]diisopropylfluorophosphate labeled the active site serine in the Mr = 33,000 chain. The first 25 amino acids of both chains were sequenced. They are identical with the sequences of the two chains of lysosomal "protective protein" which, in turn, has sequence similarity to the KEX1 gene product and carboxypeptidase Y of yeast. This protective protein complexes with beta-galactosidase and neuraminidase in lysosomes and is vitally important in maintaining their activity and stability. A defect in this protein is the cause of galactosialidosis, a severe genetic disorder. The ability of physiological stimuli (e.g. thrombin or collagen) to release the deamidase from platelets indicates that it may also be involved in the local metabolism of bioactive peptides.
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PMID:A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein". 169 76

Unicameral bone cyst fluid possesses N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, PZ-peptidase, cathepsin D, acid phosphatase, N-acetyl-beta-D galactosaminidase, and beta-galactosidase activities. The activities of lysosomal enzymes in the cyst fluid are, as a rule, higher than in the serum, whereas the total protein content is lower. The content of collagen degradation products in the cyst fluid is higher compared to the serum. In bone cavity wall tissues, the collagen content is decreased. Adenosine 3':5'-cyclic phosphate and cyclic guanosine 3,5'-monophosphate accumulate in the cyst cavity. However, in some cases, there is no correlation among the activities of lysosomal enzymes in the cyst fluid, blood serum, and cyst wall tissues. The ratios of lysosomal enzyme activities in the cyst fluid differ from those in the cyst wall tissues, cultured skin fibroblasts, and blood polymorphonuclear leucocytes. The lack of coincidence of enzymatic spectra of the cyst fluid, wall tissues, and serum is suggestive of the diversity of ways of lysosomal enzyme enter the cyst cavity, i.e., blood, cyst fluid cells, and cyst cavity walls. The cysts with different locations (i.e., active and latent cysts) have similar lysosomal lytic potentials. The presence in the cyst cavity of extracellular lysosomal enzymes and collagen degradation products testifies to the permanent corrosion of the cyst cavity walls from the inside as well as to the increase in the osmotic pressure of the cyst fluid. Lysosome destruction should be regarded as an important pathogenetic factor that requires surgical or pharmacologic correction or both in the course of bone cyst management.
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PMID:The role of lysosomes in the pathogenesis of unicameral bone cysts. 185 Mar 36

The aim of the present experiment was to determine the influence of either probiotic or antibiotic inclusion in the diets of pigs from birth on the development of enzyme activity in the small intestine. Pigs were fed on creep feed and grower diets containing either a probiotic, an antibiotic or no added growth promoter. At 7, 17, 42 and 80 d of age pigs from each treatment group were sampled to investigate the development of carbohydrase and peptidase activity in the mucosa at five sites along the small intestine. Inclusion of either the probiotic or antibiotic had a significant effect on the development of sucrase (sucrose alpha-D-glucohydrolase; EC 3.2.1.48), lactase (beta-D-galactoside galactohydrolase; EC 3.2.1.23) and tripeptidase (EC 3.4.11.4) activities before weaning but had no effect on depeptidase (EC 3.14.13.11) activity. The study of the distribution of enzyme activity along the small intestine showed significant differences between the proximal and distal sections associated with weaning.
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PMID:The influence of inclusion of either an antibiotic or a probiotic in the diet on the development of digestive enzyme activity in the pig. 211 23

In the lysosome, the glycosidases neuraminidase (EC 3.2.1.18) and beta-galactosidase (EC 3.2.1.23) are associated to a 52 kDa "protective protein" to form a large multi-enzymatic complex. Deficient synthesis or inactivation of this protective protein causes galactosialidosis, a lysosomal storage disorder in man in which both neuraminidase and beta-galactosidase activities are deficient. Since the protective protein possesses extensive sequence homology with carboxypeptidase Y (carb Y) and the KEX 1 gene product from yeast, we have used the artificial substrate N-CBZ-Phe-Leu to detect and characterize the peptidase activity of the lysosomal carboxypeptidase (carb L). Using both a purified preparation of the lysosomal multi-enzymatic complex and cultured skin fibroblasts of patients affected with galactosialidosis, we demonstrate that the 52 kDa protective protein is responsible for carb L activity. The fibroblasts of three patients affected with late infantile and juvenile galactosialidosis were found to be deficient in carb L activity (1.4% of normal mean value).
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PMID:Deficient lysosomal carboxypeptidase activity in galactosialidosis. 232 2

Gamma-Glutamyl transpeptidase (gamma-GT) was studied histochemically and biochemically in the rat epididymis after castration with or without testosterone treatment, or after hemicastration and ligation of the efferent ducts. There was a strong reaction to gamma-GT in the apical part of the epithelium in the caput epididymis, while in the corpus and cauda the reaction was confined mainly to the luminal contents. Castration caused a marked decline in epithelial gamma-GT activity within 10 days. Subsequent testosterone treatment (1 mg/day for 10 days) restored gamma-GT activity in the apical surface and lumen. After hemicastration of adult rats, and after hemicastration or ligation of the efferent ducts in immature 28-day-old rats, a small but significant (P less than 0.001) decrease was observed in gamma-GT activity in the epididymal caput compared to controls. The quantities of six other enzymes (beta-N-acetylglucosaminidase, beta-galactosidase, angiotensin-converting enzyme, alanyl amino-peptidase, dipeptidyl peptidase IV, acid phosphatase) also displayed significant changes after castration and restoration of activities by testosterone treatment. However, their distribution in the caput and cauda epididymis was more even than that of gamma-GT, and the changes after castration were less drastic. It is concluded that gamma-GT is a highly sensitive androgen-dependent secretory marker in the caput epididymis and may have an important function in sperm maturation.
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PMID:Gamma-glutamyl transpeptidase in rat epididymis: effects of castration, hemicastration and efferent duct ligation. 257 65


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