Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adult rat lung cytoplasm contains some factors which markedly stimulate adenylate cyclase activity in plasma membranes (Nijjar, M.S. Biochim. Biophys. Acta 584:43-50, 1979). Adenylate cyclase activator (ACA) was purified from rat lungs by DEAE-cellulose chromatography, preparative isoelectric focusing and by repeated high-performance liquid chromatography on a Sepharogel TSK 2000SW column. The final preparation showed about 200 fold purification in ACA activity over the original lung supernatant, and appeared to be homogeneous on the basis of its migration into a single band on SDS-polyacrylamide gel electrophoresis, and co-elution of ACA activity with protein from a gel exclusion column. ACA is an acidic (pI 4.8 +/- 0.1), heat labile, monomeric protein of 40,000 +/- 2,000 dalton molecular weight, and does not resemble calmodulin.
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PMID:Further purification and partial characterization of the rat lung cytoplasmic factors modulating adenylate cyclase activity in plasma membrane. 317 46

A five step scheme has been developed for the purification of a methyltransferase (MT) from mycelia of 3-day old Aspergillus parasiticus (SRRC 163), which catalyzes one step in the aflatoxin biosynthetic pathway. The S-adenosylmethionine (SAM) requiring MT activity is essential for the conversion of sterigmatocystin (ST) to O-methylsterigmatocystin (OMST) prior to being converted to aflatoxin B1. The purification of the MT was carried out from cell-free extracts by CDR (Cell Debris Remover, a cellulosic weak anion exchanger, Whatman) treatment, QMA ACELL, Hydroxylapatite-Ultrogel, PBE 94 chromatofocusing and FractoGel TSK HW-50F filtration chromatography. The purified enzyme was only about 0.1% of the total extractable proteins. The pI of the protein was about 5.0 as judged by chromatofocusing. Results of gel filtration chromatography indicated the approximate molecular mass of the native protein to be 160-KDa. SDS-polyacrylamide gel electrophoresis revealed two protein subunit bands of molecular masses approximately 110-KDa and 58-KDa. The molar extinction coefficient of the enzyme at 280 nm was estimated to be 7.87 X 10(4) M-1 cm-1 in 50 mM potassium phosphate buffer (pH 7.5). The reaction catalyzed by the MT was optimum at pH 7.5 and between 25-35 degrees C. The Km of the enzyme for ST and SAM was determined to be 1.8 microM and 42 microM, respectively with an estimated turnover number of the enzyme for ST of 2.2 X 10(-2) per sec.
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PMID:Purification and characterization of a methyltransferase from Aspergillus parasiticus SRRC 163 involved in aflatoxin biosynthetic pathway. 323 48

The damaging effect of an oxygen free radical generating system, i.e. ultraviolet irradiation, on human immunoglobulin G (IgG) was studied. The free radical altered IgG was analysed by a high performance liquid chromatograph equipped with a TSK G 3000 SW-column. Gel filtration of 120 min UV-irradiated IgG resulted in three clearly distinguished peaks corresponding to polymer IgG (MW greater than 500 kD), dimer IgG (MW 300 kD) and monomer IgG (MW 150 kD). Analysis of oxygen free radical altered and aggregated IgG by SDS-PAGE and subsequent silver-staining revealed inter- and intra-molecular reduction (by beta-mercaptoethanol)-resistant cross-links between IgG-molecules were formed. Comparison of amino acid analyses of native IgG with oxygen free radical aggregated polymer IgG showed significant reductions in tyrosine- (7.0%) and histidine- (6.5%) content. These findings suggest that tyrosine and histidine are involved in covalent cross-linking between IgG-molecules caused by oxygen free radicals. These alterations on IgG induced by free radical-activity might render it antigenic, and could initiate the production of rheumatoid factors (RF).
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PMID:Covalent cross-links in oxygen free radical altered human immunoglobulin G. 323 49

Cardiac sarcolemma (SL) vesicles were subjected to irradiation inactivation-target sizing analyses and gel permeation high performance liquid chromatography (HPLC) to ascertain the weight range of native Na-Ca exchange. Frozen SL vesicle preparations were irradiated by electron bombardment and assayed for Na-Ca exchange activity. When applied to classical target sizing theory, the results yielded a minimum molecular weight (Mr) of approximately 226,000 +/- 20,000 SD (n = 6). SL vesicle proteins were solubilized in 6% sodium cholate in the presence of exogenous phospholipid and fractionated by size on a TSK 30XL HPLC column. Eluted proteins were mixed 1:1 with mobile phase buffer containing 50 mg/ml soybean phospholipid and reconstituted by detergent dilution. The resulting proteoliposomes were assayed for Na-Ca exchange activity. Na-Ca exchange activity eluted in early fractions containing larger proteins as revealed by SDS-PAGE. Recovery of total protein and Na-Ca exchange activity were 91 +/- 7 and 68 +/- 11%, respectively. In the peak fraction, Na-Ca exchange specific activity increased two- to threefold compared to reconstituted controls. Compared to the elution profile of protein standards under identical column conditions, sodium cholate solubilized exchange activity had a minimum Mr of 224,000 Da. Specific 45Ca2+-binding SL proteins with Mr of 234,000, 112,000, and 90,000 Da were detected by autoradiography of proteins transferred electrophoretically to nitrocellulose. These data suggest that native cardiac Na-Ca exchange is approximately 225,000 Da or larger. The exact identification and purification of cardiac Na-Ca exchange protein(s) remains incomplete.
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PMID:Evidence for high molecular weight Na-Ca exchange in cardiac sarcolemmal vesicles. 324 56

Decidual prolactin-releasing factor (PRL-RF), a placental protein that stimulates the release of prolactin from human decidual tissue, has been purified from conditioned medium of human placental explants. The purification scheme consisted of ethanol extraction, anion exchange chromatography on DEAE-cellulose, size exclusion chromatography on Spherogel TSK-3000, and either a) immunoaffinity chromatography using an antiserum to a partially purified PRL-RF preparation or b) acetic acid-urea/SDS 2-dimensional PAGE. The apparent molecular weight of the purified releasing factor, estimated by SDS-PAGE, was 23,500 Da; and the half-maximal dose for the acute stimulation of prolactin release from human decidual cells was 0.05-0.1 ug/ml (2.2-4.4 nM).
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PMID:Purification of decidual prolactin-releasing factor, a placental protein that stimulates prolactin release from human decidual tissue. 330 79

An antihemorrhagic factor was purified from the serum of Dinodon semicarinatus, a non-venomous snake (Akamata), by a series of high performance liquid chromatographies with a TSK gel DEAE-5PW column. The purified antihemorrhagic factor showed a single band on polyacrylamide gel disc electrophoresis and inhibited the hemorrhagic activity of HR1 and HR2, the hemorrhagic factors of Trimeresurus flavoviridis Okinawa. The antihemorrhagic factor was stable from 0 degrees to 60 degrees and at pH values 2.0-11.0. The molecular weight of the factor was estimated to be 59,000 and 52,000 by a gel filtration and SDS-disc electrophoresis, respectively, suggesting that it consists of a single subunit, as we also found for the antihemorrhagic factors of the mongoose Herpestes edwardsii.
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PMID:Purification of an antihemorrhagic factor from the serum of the non-venomous snake Dinodon semicarinatus. 340 53

Prolactin (PRL) was extracted with acid-acetone from common carp (Cyprinus carpio) pituitary glands and purified by gel filtration on Sephadex G-75, ion-exchange chromatography on DEAE-cellulose, and reversed-phase high-performance liquid chromatography (HPLC) on TSK-gel TMS 250 with a yield of 0.7 mg/g wet tissue. At each stage of purification, fractions were monitored by HPLC on TSK-gel ODS 120T and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Carp PRL was almost equipotent with ovine PRL in retaining plasma Na concentrations in the hypophysectomized killifish, Fundulus heteroclitus. Immunocytochemistry at both the light and electron microscopic levels revealed that carp PRL antiserum specifically stained cells in the goldfish rostral pars distalis. No cross reaction with putative growth hormone (GH) cells in the proximal pars distalis was observed. The specificity of the carp PRL antiserum was confirmed by immunoblot studies. Although immunostaining of both carp and salmon PRL was observed, there was no cross reaction to GHs from these species. Carp PRL had a sole N-terminal residue of valine, a molecular weight of 23 kDa in SDS-PAGE, and an isoelectric point of 7.3 by gel electrofocusing. Based on these results, together with the knowledge of physicochemical properties of salmon and tilapia PRLs, we propose a standard procedure for isolation of fish PRLs.
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PMID:Isolation and characterization of carp prolactin. 341 16

An inhibitor of neutral proteinases was isolated from the cytosol of bovine leukocytes by anion exchange chromatography on Mono Q and gel filtration on a HPLC TSK column. The gel filtration resulted in two fractions with inhibitory activity which could be identified by sodium dodecyl sulphate-poly-acrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions as dimer and monomer of the inhibitor. The latter was shown to be homogeneous in SDS-PAGE with an apparent molecular mass of 40 kDa, with calibrated HPLC a molecular mass of 36.5 kDa has been determined. Isoelectric focusing followed by Western blot analysis revealed four bands in the pH range of 5.0 to 5.9. The inhibitor was found in bovine polymorphonuclear neutrophils (PMN), whereas lymphocytes and monocytes lacked this protein. No immunological cross-reactivity between the described cell-derived PMN-inhibitor (PMN-I) and alpha 1-proteinase inhibitor was detectable. The mechanism of inhibition for the serine proteinases chymotrypsin, trypsin, pancreatic elastase and leukocyte elastase was studied. PMN-I could not bind to PMS-chymotrypsin. The reaction of the serine proteinases with the PMN-I was characterized by the determination of the association rate constant kon.
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PMID:Neutral proteinase inhibitors in PMN leukocytes. I. Purification and characterization of a neutral proteinase inhibitor from bovine neutrophils. 342 3

Whey is a suitable source of immunoglobulins and lactoferrin to enrich infant formulas. Gel filtration on Sephacryl S-300 and on Fractogel TSK HW-55 was used to isolate immunoglobulins from colostral whey, acid whey, and Cheddar cheese whey. The SDS-PAGE and immunoelectrophoresis techniques indicated that the purity of the fractions from fractionation on Sephacryl S-300 was better than that by fractionation on TSK HW-55 column. Biological activity of fractions from the Sephacryl S-300 column as assessed by immunochemical analysis was 99, 83.3, and 92% for colostral, acid, and sweet wheys. The well-proven antimicrobial agent, lactoferrin, was isolated from sweet whey by heparin-attached Sepharose. Lactoferrin selectively adsorbed to the column was subsequently eluted with 5 mM Veronal-HCl containing .5 M NaCl, pH 7.4. Purity of the isolated protein was confirmed by SDS-PAGE and immunoelectrophoresis.
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PMID:Isolation of bovine immunoglobulins and lactoferrin from whey proteins by gel filtration techniques. 344 4

A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystallins were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.
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PMID:Biochemical comparison of epsilon [correction of gamma]-crystallins from duck and frog eye lenses. 348 58


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