Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A hitherto unknown alpha-neurotoxin, alpha-agkistrodotoxin, was isolated from the venom of the pit viper Agkistrodon halys (Pallas). It's molecular weight was approx. 8000 +/- 80 (SDS-polyacrylamide electrophoresis). The toxin crossreacted with antiserum directed against alpha-bungarotoxin and inhibited binding of 125I-alpha-bungarotoxin to the nicotinic acetylcholine receptor of cultured myotubes (IC50 = 2 X 10(-9) M). The association and dissociation rates were 4.85 X 10(5) per mole per min and 3.55 X 10(-4) per min, respectively, giving a Kd of 7.3 X 10(-10) M. The toxin also inhibited carbachol-induced influx of cations through the nAChR (IC50 = 6 X 10(-8) M).
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PMID:Isolation and pharmacological characterization of a new alpha-neurotoxin (alpha-AgTx) from venom of the viper Agkistrodon halys (Pallas). 343

Three molecular species of apolipophorin III were purified from adult locust hemolymph by gel filtration and ion-exchange chromatography, and named apo-III-a, apo-III-b, and apo-III-c, respectively. They were indistinguishable by SDS-polyacrylamide gel electrophoresis, immunodiffusion, and in amino acid composition; however, they had different isoelectric points (5.43 for a, 5.11 for b, and 4.98 for c) and, therefore, could be separated by native- or urea-gel electrophoresis. All three apo-IIIs were glycoproteins and contained fucose, mannose, and glucosamine. The total sugar content amounted to about 11% for each of the three apo-IIIs. The molecular weight of apo-III determined by SDS-polyacrylamide gel electrophoresis was approximately 20,000, almost equivalent to the native molecular weight (approximately 19,000) estimated by the sedimentation-equilibrium method. This indicated that the locust apo-III exists in hemolymph as a monomeric form. It was demonstrated that a total 9 moles of apo-III (2 moles apo-III-a, 6 moles apo-III-b, and 1 mole apo-III-c) associate with each mole of lipophorin in response to the action of locust adipokinetic hormone.
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PMID:Apolipophorin III in locusts: purification and characterization. 352 83

Two species of T-kininogen which release T-kinin (Ile-Ser-bradykinin) have been purified from plasma of rats treated with Freund's complete adjuvant. The molecular weight was estimated to be 69,000 for either T-kininogen I and II by SDS-polyacrylamide gel electrophoresis. Trypsin released one mole of T-kinin from one mole of either T-kininogen, but glandular kallikrein, including rat urinary and rat submandibular gland kallikreins and human urinary kallikrein, did not release any kinin from T-kininogens. Cathepsin D, which was purified from rat liver, released T-kinin from T-kininogens at pH 4.0. These results indicate that rat plasma contains two types of T-kininogen which differ from high molecular weight and low molecular weight kininogens.
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PMID:Isolation and properties of two rat plasma T-kininogens. 354 20

Human plasma glutathione peroxidase (GPx) was purified to homogeneity by ammonium sulfate fractionation, gel filtration on Sephadex G-150, chromatography on DEAE Sephacel, chromatofocusing with polybuffer, and gel filtration with Sephadex G-75. This isolation resulted in about 5,400-fold purification of the enzyme with a 32% yield in enzyme activity. The final preparation had a specific activity of about 28 units (mmoles NADPH oxidized) per milligram of protein. Determination of selenium on the purified enzyme revealed a content of 3.8 g atoms per mole GPx. Gel electrophoresis using SDS with standard proteins revealed a molecular weight of about 23,000 for the subunits, which would indicate a molecular weight of about 92,000 for the native enzyme. Amino acid analyses of the purified GPx indicated aspartate, glutamate, proline, glycine, alanine, and leucine as the predominant amino acids and cysteine, methionine, tryptophan, and histidine as the minor amino acids.
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PMID:Properties of glutathione peroxidase isolated from human plasma. 366 26

A protease inhibitor was purified from the African marama bean (Tylosema esculenturm). The inhibitor is present in large amounts, representing about 10.5% of the total protein. The molecular weight is slightly larger than soybean trypsin inhibitor and was estimated at 23,000 by SDS-gel electrophoresis or 24,500 by amino acid analysis. The amino acid composition was atypical of most other plant inhibitors with a cysteine content of only one or possibly two residues/mole and a blocked amino terminus. Inhibition studies indicated virtually no inhibition of chymotrypsin activity. Elastase, however, was inhibited to the same extent as trypsin, requiring about 2 moles of inhibitor for complete inhibition of the enzyme.
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PMID:Isolation and characterization of a proteinase inhibitor from marama beans. 385 Jun 10

A monoclonal antibody (MAb NKI/C-3) produced against a purified membrane preparation of human melanoma cells reacts preferentially with sections of formaldehyde-fixed and paraffin-embedded tissues of melanoma, nevocellular nevi, carcinoids and medullary carcinomas of the thyroid. NKI/C-3 did not react with basal-cell carcinoma, brain tissue or brain tumors, and in only 14/196 other tumors was a clear cross-reactivity observed, e.g. with prostate carcinomas and a minority of primary breast, ovarian, lung and clear-cell carcinomas. This antibody was used in an immuno-electron microscopic study for the cellular localization of the antigen. The antigen was dispersed in the cytoplasm of melanoma cells, and more concentrated inside vacuoles and sometimes also on the melanosomes. Occasionally, the antigen was seen on the cell surface. The nature of the antigen was determined in an enzyme immunoassay (EIA). It was found that the antigen is a glycoprotein with a disulfide-dependent configuration that is essential for recognition by the MAb. The antigen was distributed heterogeneously during gel filtration as well as during SDS-polyacrylamide gel electrophoresis in the region of 25-110 kd proteins. A purified antigen preparation that was obtained after affinity chromatography on a column of MAb NKI/C-3 linked to Sepharose 4B contained a carbohydrate:protein ratio of 1:3.5.
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PMID:Biochemical characterization and cellular localization of a formalin-resistant melanoma-associated antigen reacting with monoclonal antibody NKI/C-3. 388 81

Aromatase cytochrome P-450 has been purified from human placenta to homogeneity, as demonstrated by electrophoresis on polyacrylamide gels with SDS, and by double diffusion against an antibody raised in rabbits. The enzyme converts androstenedione to estrone (Vmax 13.3 n moles/min/n mole P-450; Km 30 microM) and testosterone to estradiol. Aromatase activity requires P-450, P-450 reductase and NADPH. Enzyme activity is inhibited by anti-aromatase antibodies and by 4-hydroxyandrostenedione. The enzyme shows a molecular weight of 55,000, is extremely unstable and spontaneously forms P-420 with a half-life of 2.5 days.
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PMID:Purification to homogeneity of aromatase from human placenta. 394 46

A specific precipitating antibody against chicken gizzard myosin light chain kinase (MLCK) has been produced in rabbits. The antibody inhibited enzyme activity in a dose-dependent manner with 11 moles of antibody required to inhibit 80% of the activity of one mole MLCK. Crude homogenates from various chicken tissues were analyzed by SDS-polyacrylamide gel electrophoresis, and the proteins were transferred onto nitrocellulose sheets and reacted with antibody. In each case, the antibody bound to only one protein with a molecular weight of approximately 130,000. These data suggest the MLCK present in all types of muscle as well as non-muscle tissues is of the same molecular weight. Indirect immunofluorescent microscopy of non-muscle tissue culture cells revealed MLCK to be localized in the spindle apparatus and midbody of mitotic cells and on the stress fibers and in the nucleolus of interphase cells. The nucleolar localization was confirmed by electron microscopy and shown to be restricted to the fibrillar region. In myofibrils isolated from skeletal and cardiac muscle, anti-MLCK decorated the actin-containing I bands of the sarcomere. These results are consistent with the suggestion that MLCK and calmodulin are intermediates in the regulation of cell motility by calcium.
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PMID:Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. 610 Nov 99

Monoclonal antibodies against human plasminogen activator urokinase have been produced. A G62 hybridoma-producing antibody (IgG) was purified on a DEAE-cellulose column, and it proved useful for the measurement, identification and purification of antigens that had approximate molecular weights of 55- and 33-Kdaltons. For immunochemical measurements and purification, a competitive enzyme-linked immunosorbent assay (ELISA) and affinity chromatography using antibody-immobilized Sepharose 4B were developed. The ELISA has sensitivity to 20 p mole antigen molecules. The binding capacity of the antigen on the affinity column was evaluated on SDS-polyacrylamide slab gels as well as by fibrin autography and ELISA. Results showed that there was quantitative purification with no loss of enzyme activity in the one-step procedure. Western blotting and affinity binding showed antigenic bands with apparent molecular weights of 55- and 33-Kdaltons. Because the 55-Kdalton form contains 33- and 22-Kdalton components connected by a disulfide bond, the epitope domain is present on the 33-Kdalton chain. Using this antibody, we examined human kidney sections by direct immunofluorescence to locate the antigen. It was found in epithelial cells convoluted segments, in glomerulus cells and in capillary endothelial cells, evidence that renal tubular cells synthesize the antigen which then is secreted in urine.
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PMID:A monoclonal antibody against human urokinase: characterization of the epitope and its localization in human kidney. 620 21

A 10-yr-old female presented with cerebriform tumors covering the plantar surfaces of both feet. Histologically, the lesions consisted of thick collagen fibers and the content of collagen per surface area of skin was increased about 8-fold. Examination of the collagen by SDS-polyacrylamide gel electrophoresis, after limited pepsin proteolysis, showed that the lesions consisted almost exclusively of type I collagen, the predominant collagen type in human skin. Thus, a diagnosis of connective tissue nevi of the collagen type was made. Fibroblast cultures were established from the affected and normal-appearing areas of the skin, and examined for the rate of collagen synthesis, production of collagenase and growth kinetics of the cells. Cell cultures derived from the lesion and from control skin synthesized procollagen at the same rate and in a normal type I/type III procollagen ratio. However, the production of enzymatically active and immunologically detectable collagenase was reduced by 70-82% in the cultures derived from the lesion as compared to controls (p less than 0.005). Fibroblasts derived from the lesions also displayed a mean population doubling time of 1.17 +/- 0.08 days compared to 1.83 +/- 0.24 and 1.92 +/- 0.09 days for control cell strains and cells derived from normal skin of the patient, respectively (p less than 0.025). These results suggest that the excessive deposition of collagen in this case may have resulted from decreased local degradation of collagen. Enhanced proliferative capacity of the regional fibroblasts may have contributed to the accumulation of collagen in these lesions.
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PMID:Decreased collagenase production by regional fibroblasts cultured from skin of a patient with connective tissue nevi of the collagen type. 627 72


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