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)

Fibronectin is a glycoprotein found in plasma (cold-insoluble globulin), connective tissues, and cultures of fibroblasts and astroglial cells. This paper describes the identification of fibronectin in human CSF. Fibronectin in CSF was immunologically indistinguishable from the plasma form, as shown by double-diffusion analysis and by radioimmunoassay specific for fibronectin. Fibronectin was isolated from human CSF by affinity chromatography on Sepharose-coupled gelatin and was further analyzed by SDS-polyacrylamide gel electrophoresis. It showed a polypeptide band similar to that of plasma fibronectin. The fibronectin concentration in CSF of 17 neurological outpatients without demonstrable organic lesion in the CNS was 3.0 +/- 1.6 microgram/ml (mean +/- S.D.) which is about 0.6% of total CSF protein. In CSF of 11 MS patients, the concentration was significantly (p less than 0.005) lower (1.6 +/- 0.2 microgram/ml). Of patients with brain tumors, seven had very low levels, three were normal, and two had very high levels. The cause for the low levels in MS and tumor patients is not known.
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PMID:Demonstration of fibronectin in human cerebrospinal fluid. 10 31

Immunochemical and double labeling experiments were used to demonstrate that at least two out of three brain cytoplasmic proteins, whose metabolism is markedly influenced by behavior, are products which are secreted into the extracellular fluid (ECF) of goldfish brain. Even after 1 h of labeling, the extracts of goldfish brains with 0.32 M sucrose were found to contain highly labeled proteins. Electrophoretic analyses of the proteins, on SDS polyacrylamide gels, indicated that an increased incorporation of [3H]valine occurs for trained animals as compared to untrained controls ([14C]valine) at specific protein bands migrating at 32,000 and 26,000 daltons. The proteins in the ECF gave identical precipitin bands to goldfish brain proteins whose metabolism was responsive to the acquisition of new patterns of behavior and to proteins in CSF. These results are consistant with the hypothesis that the cells which contain the proteins and whose location in the ependymal zone was determined by immunohistochemistry can secrete the products into ECF. It is therefore quite possible that the functional sites of the proteins are away from the locus of their synthesis.
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PMID:Brain metabolism and the acquisition of new behaviors. III. Evidence for secretion of two proteins into the brain extracellular fluid after training. 10 29

CSF was prepared by the growth of L cells in serum-free culture medium. This conditioned medium was subjected to a six-step purification schedule which included ultrafiltration, alcohol precipitation, and separation by DEAE-cellulose, Con A-Sepharose, Sephadex G-150, and sucrose density-gradient centrifugation. The resultant CSF was 1000-fold purified with 50% to 70% recovery of the starting activity. Granulocyte and macrophage colony formation was detected with 5 x 10(-12M CSF; maximum colonies were obtained with 3 ng per marrow culture. Two major peaks of activity were obtained; one was nonadherent to Con A, whereas the other was bound and specifically eluted with alpha-methylglucoside. Both fractions contained carbohydrate residues as they stained avidly with PAS, were inactivated by periodate, and showed altered electrophoretic mobility after treatment with neuraminidase. Following iodination, each purified fraction migrated in a single band in SDS-acrylamide gels. The molecular weight was estimated as 65,000 to 70,000 daltons. Following reduction with mercaptoethanol, the CSF fractions were reduced into subunits with molecular weights of approximately 35,000. These studies confirm the glycoprotein nature and subunit composition of L cell CSF. The methods described herein are useful for the purification of both the Con A-adherent and con A-nonadherent forms of CSF.
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PMID:Purification and properties of L cell-derived colony-stimulating factor. 31 66

Peripheral blood eosinophils from normal healthy subjects were isolated on a Percoll gradient and were incubated with [32P] orthophosphoric acid. 32P-labeled eosinophils were washed and stimulated with GM-CSF under different conditions. After reaction was stopped, SDS/PAG electrophoresis was performed along with autoradiographs to determine the incorporation of 32P into proteins. GM-CSF-stimulated eosinophils produced an increase of 32P incorporation into the bands in the 31 kDa and 35 kDa areas after 30 sec and 1 min of stimulation. The increase of 32P incorporation was dependent on Mg2+ concentration and temperature, suggesting that proteins in the eosinophils with apparent molecular weights of 31 kDa and 35 kDa can be phosphorylated with the stimulation of GM-CSF.
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PMID:[Protein phosphorylations in granulocyte/macrophage colony-stimulating factor-stimulated human peripheral blood eosinophils]. 129 Apr 14

Clinical effects of KRN8601 (recombinant human granulocyte colony-stimulating factor:rhG-CSF) were studied in 26 patients with chronic neutropenia including 4 Kostmann's disease, 1 Shwachman's syndrome, 1 Lonsdale's syndrome, 1 glycogen storage disease Ib-associated, 6 chronic benign, 5 chronic hypoplastic, 2 cyclic, 4 autoimmune and 2 miscellaneous neutropenia. The patients were given rhG-CSF intravenously at doses of 20-540 micrograms/m2 or subcutaneously at doses 20-400 micrograms/m2, over the periods of 2-32 weeks. Increases in neutrophil counts occurred after rhG-CSF administration in 23 of the 26 patients. Patients with Kostmann's disease, Shwachman's syndrome and chronic hypoplastic neutropenia responded poorly compared to patients with other types of neutropenia. There were no serious side effects which caused interruption of the study. These results indicated a beneficial effect of KRN8601 in various types of chronic neutropenia.
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PMID:[Clinical evaluation of effects of KRN8601 (rhG-CSF) on neutropenia]. 137 11

A total of 23 isolates of Borrelia burgdorferi were characterized by SDS-PAGE and immunoblot analysis. One isolate came from the CSF of a Lyme neuro-borreliosis patient in Valais (Switzerland) and 22 were tick isolates (2 from I. dammini of Shelter Island, USA and 20 from I. ricinus of Valais, Switzerland). Based on the electrophoretic mobility of outer surface proteins (OspA and OspB), four groups of B. burgdorferi could be defined. Group I isolates possess an OspA of 31 KD and an OspB of 34 KD. The group II isolate showed an OspA of 32 KD and OspB of 35 KD. Group III isolates have a 33 KD OspA and group IV a 33.5 KD OspA. This classification was confirmed by the reactivity of a monoclonal antibody (D6) to a 12 KD antigen that was recognized in group III only. A Lyme patient's serum showed a 2-band pattern (10 and 13 KD) for group I and a one-band pattern (12 KD) for the other 3 groups. Therefore OspA, OspB and other proteins of low molecular weight (10, 12, and 13 KD) seem to be important keys for the classification of B. burgdorferi isolates. This typing system correlates with genetic analysis.
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PMID:Polymorphism of outer surface proteins of Borrelia burgdorferi as a tool for classification. 152 Sep 66

Citrobacter diversus brain abscess occurred in two infants in Aberdeen, 5 months apart. These are the first reported cases of this condition in the UK since 1976. Restriction endonuclease analysis with SacI enzyme showed blood and CSF isolates from both patients to be identical and different from 10 other clinical isolates of C. diversus and one C. amalonaticus strain. Furthermore, isolates of C. diversus from patients belonged to biotype "d" whereas control isolates were of biotypes "a" or "e". Because both infants attended the same central and peripheral maternity units, this raised suspicions of long term contamination of the hospital environment by this organism. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of whole-cell proteins and immunoblotting with normal human serum were remarkably homogeneous for all 13 C. diversus strains and thus were not useful for typing. However, the only C. amalonaticus strain was clearly differentiated from C. diversus strains by SDS-PAGE. Management of the infants included multiple intravenous antibiotic therapy for 4-6 weeks and repeated computerised tomography (CT) scanning and drainage of the abscess cavity. Both children survived albeit with some minor degree of brain damage.
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PMID:Citrobacter diversus brain abscess: case reports and molecular epidemiology. 156 Apr 49

Peripheral granulocytes from rheumatoid arthritis and reactive arthritis patients were recently found to express higher levels of a newly defined Ag, termed M6, in comparison to granulocytes from healthy subjects. We present here the molecular characterization of M6 Ag and show that it is a novel human leukocyte activation-associated cell surface glycoprotein. Peripheral lymphocytes do not significantly express M6 Ag, however, it appears upon 3-day PHA-activated T blasts. On monocytes, which constitutively express M6 Ag, it is down-regulated on day 1 but re-induced on day 3 of granulocyte-macrophage CSF stimulation. SDS-PAGE analysis of M6 immunoprecipitates shows a single band of 54 kDa under nonreducing conditions that shifts to 65 kDa under reducing conditions. Endoglycosidase F treatment of M6 immunoprecipitate reveals that 50% of the M6 molecule is composed of N-linked carbohydrates. By modifying the COS cell cloning strategy, we have isolated cDNA clones encoding M6 Ag. M6 cDNA hybridizes with a single mRNA transcript of approximately 1.7 kb in Northern blotting. Comparison analysis of the M6 sequence indicates that M6 Ag is a member of the Ig superfamily and the species homologue of rat OX-47 Ag, mouse basigin (gp42), and chicken HT7 molecule. The highly conserved remarkable transmembrane domain suggests that the M6 Ag may be a component of a multichain complex in the plasma membrane.
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PMID:Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. 163 73

Surgically collected cystic fluid of Taenia solium metacestodes from patients of intracranial cystic lesion were compared in their protein composition with those from naturally infected pigs in Cheju Do, Korea and Ecuador. In non-denaturing discontinuous-polyacrylamide gel electrophoresis (disc-PAGE), no discernible differences were recognized in banding patterns between the cystic fluids from Cheju Do and Ecuador, and between the cystic fluids from pigs and human lesions except wider bands that corresponded to human albumin and gamma-globulin (in 4 of 9 patients). In reducing SDS-PAGE, bands in the cystic fluid from Ecuador showed the same banding pattern with that from Cheju Do but two bands of 21 and 17 kDa were stained darker. Cystic fluids from patients revealed the same protein compositions of the major protein bands of 94, 64, 15, 10 and 7 kDa as in the cystic fluid of pig origin, but human albumin (66 kDa), heavy and light chains of gamma globulin (55 and 22.5 kDa) were contaminated in 4 of 9 cystic fluids. Human CSF proteins seem to have been contaminated during cystic fluid collection. In any cystic fluid from patients, the major protein component was 150 kDa which was subdivided into 15, 10 and 7 kDa in reducing SDS-PAGE.
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PMID:Component proteins in cystic fluid of Taenia solium metacestodes collected surgically from neurocysticercosis patients. 170 89

Cerebrospinal fluid insulin-like growth factor binding proteins (CSF IGFBPs) characteristically have a preferential affinity for IGF-II, which is largely accounted for by a 32-30 kDa IGFBP(Ka = 10(11) M-1) previously purified from human CSF, with an N-terminal sequence unlike any other IGFBP identified at the time. We have now used procedure (including ammonium sulphate precipitation, acidic gel filtration, affinity chromatography and reverse phase chromatography) and purified three further IGFBPs to homogeneity from child CSF. Apart from the 32-30-kDa form, the predominant IGFBP in CSF is a 34-kDa form (non-reduced in SDS-polyacrylamide gel electrophoresis). Like the 32-30-kDa IGFBP, it has a preferential affinity for IGF-II (Ka = 2 x 10(10) M-1). Its N-terminus, Phe-Arg-(/)-Pro-Pro-(/)-Thr-Pro-Glu-Arg-Arg-(/)-Gly-Pro-Pro-Pro-Val, corresponds to that deduced for IGFBP-2, except for the first three residues which were not found in the CSF IGFBP. Another form, of 30 kDa, has an N-terminus identical to IGFBP-3's over the first 18 residues determined and seems to be an altered form of IGFBP-3. A third minor species, of 22 kDa, with a preferential affinity for IGF-II similar to that of the 34-kDa IGFBP, has an N-terminal sequence, (/)-(/)-Asp-Ser-Phe-Val-Pro-(/)-Glu-Pro-Ser-Asp-Glu-Lys-Ala-Leu-Ser-(/)- (/)-Pro, which bears some analogy with those of other known human IGFBPs, particularly IGFBP-3 (7 homologous residues), and appears to be related to, but distinct from, other IGFBP species.
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PMID:Purification from human cerebrospinal fluid of insulin-like growth factor binding proteins (IGFBPs). Isolation of IGFBP-2, an altered form of IGFBP-3 and a new IGFBP species. 172 37


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