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)

Polypeptides in the dorsal root ganglion (L5) of the adult rat were radioactively labeled, and components slowly migrating in the sciatic nerve (peripheral axons) and dorsal root (central axons) were analyzed, using SDS-polyacrylamide slab gel electrophoresis and fluorography. In particular, the transport rates and amounts of six major polypeptides, i.e., the triplet (reference 15; with mol wts of 200,000, 160,000, and 68,000 daltons), alpha- and beta-tubulins and actin were compared between the two axon branches. In peripheral axons, fronts of the triplet, tubulins, and actin migrate at 2-3 mm/d, 9-13 mm/d and approximately 19 mm/d, respectively. The corresponding values in central axons are 1-2 mm/d, 3-4 mm/d, and approximately 4 mm/d, indicating an obvious asymmetry in the transport rate between the two branches of bifurcating axons. A greater amount of labeled triplet, tubulins, and actin each is found to migrate in peripheral than in central axons. Another striking aspect of asymmetry between the two branches relates to the tubulins/triplet ratio which is significantly higher in the peripheral branch. Considerable proportions of radioactivities associated with tubulins and actin in the ganglion are nonmigratory, which are thought to derive mostly from periaxonal satellite cells. In contrast, most if not all of the labeled triplet is migratory, suggesting a virtual absence of triplet polypeptides in satellite cells. The possible significance of peripheral-central inequalities in slow axoplasmic transport is discussed from the viewpoints of axon volume and axonal outgrowth.
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PMID:Slowly migrating axonal polypeptides. Inequalities in their rate and amount of transport between two branches of bifurcating axons. 9 50

Chancroid is a sexually transmitted diseased caused by Haemophilus ducreyi. The pathological manifestations of chancroid are unique among Haemophilus species and the virulence factors of H. ducreyi that account for these features have not been identified. Some of these virulence factors may be unique components of H. ducreyi, but attempts to identify H. ducreyi-specific components have been unsuccessful. Four polypeptides--A, B, C and D of 83, 77, 56 and 28 kDa, respectively--were identified with a panel of nine H. ducreyi-specific monoclonal antibodies (MAbs). Polypeptide C was one of the five major proteins in H. ducreyi and demonstrated micro-heterogeneity in SDS-PAGE. Polypeptides A, B and D were present in only small amounts in whole-cell lysates of H. ducreyi. The relative amounts of A and B varied, suggesting that they may be precursor molecules. The unique polypeptides C and D were not exposed on the surface. Polypeptide C was highly soluble and did not appear to be membrane-bound, whereas polypeptide D appeared to partition with the cytoplasmic membrane and was soluble in Sarkosyl. All four polypeptides appeared to be unique to H. ducreyi since MAbs directed against them did not cross-react with H. influenzae, H. parainfluenzae or Neisseria gonorrhoeae. The mol. wts of all of these polypeptides were conserved throughout 35 clinical isolates collected from 15 cities in eight countries and one reference strain of H. ducreyi that were tested.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of highly conserved and species-specific polypeptides of Haemophilus ducreyi. 128 Dec 34

Hepatic microsomes of female F344 rats were capable of N,O-acyltransfer of N-hydroxy-N-acetyl-2-aminofluorene (N-OH-AAF) and N-hydroxy-N-formyl-2-aminofluorene (N-OH-FAF), N-deacetylation of N-OH-AAF and N-acetyl-2-aminofluorene (2-AAF), and O-deacetylation of 4-nitrophenyl acetate (NPA). The activity for N,O-acyltransfer of N-OH-FAF was approximately 20 times greater than that of N-OH-AAF. These microsomal activities were inducible by phenobarbital and were inhibitible by paraoxon. Four distinct N,O-acyltransferases were purified from solubilized hepatic microsomes of phenobarbital pretreated rats. These enzymes were purified to homogeneity, as judged by SDS-PAGE and analytical IEF. Their pIs were approximately 5.0, 5.5, 6.0 and 6.5 and their mol. wts were approximately 60, 61, 180 (a homotrimer of 59 kDa) and 60 kDa respectively. All the enzymes catalyzed the N,O-acyltransfer of N-OH-FAF, the N-deacetylation of N-OH-AAF and 2-AAF and the O-deacetylation of NPA. Among these four enzymes, the hydrolysis of NPA was best catalyzed by pI 6.5 protein, of 2-AAF by the pI 5.5 protein, and of N-OH-AAF by the pI 5.0 protein. The pI 5.5 and pI 6.5 proteins were equally active for N,O-acyltransferase and were more active than the other enzymes. The present study demonstrates that rat hepatic microsomal activities of N,O-acyltransfer, N-deacetylation and O-deacetylation are attributable to the same enzymes.
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PMID:Purification and characterization of rat hepatic microsomal N,O-acyltransferases. 142 70

Two fibrinolytic enzymes, jararafibrase I and jararafibrase II, were purified from Bothrops jararaca venom. The purified jararafibrase I and jararafibrase II ran as single protein bands on analytical polyacrylamide gel electrophoresis and had mol. wts of 47,000 +/- 2000 and 21,400 +/- 500, respectively, by SDS-polyacrylamide gel electrophoresis. The isoelectric points of jararafibrase I and jararafibrase II were 4.6 and 6.5, respectively. The specific activities of jararafibrase I and jararafibrase II were 2.2 units/mg protein and 6.3 units/mg protein, respectively. Both enzymes exhibited no detectable plasminogen activating activity. The activity of the enzymes was completely inhibited by 1,10-phenanthroline and ethylenediaminetetraacetate, suggesting that both enzymes were metalloproteinases. Jararafibrase I and jararafibrase II had single-chain protein compositions, and the amino acid sequence up to the 49th amino acid from the NH2-terminal of jararafibrase II was: Leu-Pro-Glu-His-Gln-Arg-Tyr-Ile-Glu-Leu-Phe-Ile-Val-Val-Asp-His-Gly-Met- Phe-Met-Lys-Tyr-Asn-Gly-Asn-Ser-Asp-Lys-Ile-Arg-Arg-Arg-Ile-His-Gln- Met-Val-Asn-Ile-Met-Lys-X-Ala-Tyr-Arg-Tyr-Leu-Tyr-Ile-(X = not confirmed).
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PMID:Purification and characterization of two fibrinolytic enzymes from Bothrops jararaca (jararaca) venom. 152 77

Two hundred and ninety-four serum specimens from 248 subjects, whose complement fixation (CF) titres to Mycoplasma pneumoniae were known, were further investigated by IgG immunoblotting. After analysis of M. pneumoniae proteins by SDS-PAGE, nine polypeptides (p) with mol. wts of 180-43 Kda were selected for immunoblotting studies. Antibodies to M. pneumoniae measured by immunoblotting appeared progressively with age; most subjects more than 19 years old gave positive results. For most of the polypeptides, there was an increase in the frequency of band detection when the CF titres were higher. Furthermore, paired serum specimens from 10 patients with M. pneumoniae infection, as demonstrated by a rise in CF antibody titre, were tested for IgG blotting patterns. Generally, p180 (the P1 adhesin of M. pneumoniae), p172 and p84 were shown to be the dominant targets of the immune response to this organism and may have diagnostic value.
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PMID:Immunoblotting patterns with Mycoplasma pneumoniae of serum specimens from infected and non-infected subjects. 158 85

Studies were carried out in order to confirm and extend knowledge of the physico-chemical properties of an allergenic material found in the pollen of the olive tree (Olea europea). The sera from 88% of patients who were sensitive to olive pollen contained IgE that reacted with a 19,000 Mr component and many also reacted to a 17,000 Mr band as shown by SDS-PAGE immunoblotting. A monoclonal antibody (OL-1) produced to the 19,000 Mr component also reacted with the 17,000 Mr band, and with bands at 21,000 and 41,000 under non-reduced conditions. HPLC separation followed by SDS-PAGE and immunoblotting of the fractions indicated that the allergen fraction from which the 19,000 and 17,000 components were derived had a mol. wt between 50 and 60 kD. Isoelectricfocusing followed by immunoblotting and development with (OL-1) indicated heterogeneity of the allergen with respect to pI values. Two of the strongest components of the six identified which reacted with (OL-1) had pIs of about 5.0 and 6.0 confirming the published data. The study therefore showed that olive pollen contains a number of allergenic components, with various mol. wts and pI values, with some epitopes in common, which may in the native state be bound together or aggregated.
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PMID:Heterogeneity of a major allergen from olive (Olea europea) pollen. 169 44

1. alpha-L-Fucosidase was purified ca 10,889-fold to homogeneity from Penaeus monodon, with a final spec. act. of 31,250 U/mg of protein. 2. By using SDS-polyacrylamide gel electrophoresis, the monomers of shrimp alpha-L-fucosidase were discovered to have mol. wts of 63,000 and those of human placental enzyme, 46,000 and 20,000. Since the active shrimp alpha-L-fucosidase was found to have a mol. wt of 233,000 by Superose 12 FPLC, it was concluded that the purified shrimp enzyme was tetrameric. 3. In contrast to the discovery of thermolability with human placental alpha-L-fucosidase, the shrimp enzyme was found to be stable to heating at 65 degrees C for 10 min. 4. The shrimp alpha-L-fucosidase has an isoelectric point (pI) of 8.5, but the human placental enzyme has a pI of 4.0. The shrimp enzyme was sialyated. 5. The shrimp alpha-L-fucosidase has a pH optimum at 5.5 and its Km was 22.2 microM with 4-methyl-umbelliferyl-alpha-L-fucopyranoside as substrate. The human enzyme has a broad pH optimum between 5.0 and 6.5.
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PMID:The basic isoelectric form of alpha-L-fucosidase from the hepatopancreas of the shrimp Penaeus monodon (Crustacea: Decapoda). 176 18

1. The lethal factor of the stonefish (Synanceja horrida) venom, designated as the stonustoxin, was purified to homogeneity by a two-step procedure on Sephacryl S-200 High Resolution (HR) gel permeation and DEAE Bio-Gel A anion exchange chromatography. 2. Stonustoxin has a native mol. wt of 148,000 and an isoelectric point of 6.9. 3. SDS-polyacrylamide gel electrophoresis revealed two subunits (designated alpha and beta) with mol. wts of 71,000 and 79,000, respectively. 4. The amino acid composition of both subunits and the N-terminal amino acid sequence of the beta subunit were also determined. 5. Purified stonustoxin had an LD50 of 0.017 microgram/g which is 22-fold more potent than that of the crude venom. 6. The toxin exhibited potent haemolytic activity in vitro and edema-inducing activity with a minimum edema dose (MED) of 0.15 micrograms in mouse paw. The edema effect was not antagonized by diphenhydramine.
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PMID:Purification and partial characterization of stonustoxin (lethal factor) from Synanceja horrida venom. 179 Jun 72

The venoms from central Asian snakes (Echis carinatus, Echis multisquamatus, Vipera ursini, Vipera lebetina, Agkistrodon halys halys and Naja naja oxiana) contain several enzymes with amidolytic- and procoagulant activity. We have characterized the activities and the mol. wts of the venom enzymes that are able to convert a number of commercially available chromogenic substrates for activated coagulation factors. The chromogenic substrate cleavage patterns obtained for the crude venoms may be helpful tools in the further identification of venom fractions and venom enzymes with procoagulant activity. The crude venoms were also tested for their ability to clot fibrinogen, to lyse fibrin polymers and to activate the coagulation factors prothrombin, factor X and factor V. The products of venom-catalyzed coagulation factor activation were structurally characterized by SDS gel electrophoresis and were compared with activated coagulation factors that are generated under physiological conditions.
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PMID:Procoagulant activities in venoms from central Asian snakes. 183 Jul 5

Mugwort (Artemisia vulgaris L.) pollen allergens, separated by SDS-PAGE or IEF, were identified after transfer to NCM by incubation with a panel of sera from 16 patients with clinical mugwort pollen allergy, followed by [125I]anti-IgE and autoradiography. Of the at least 23 components separated by SDS-PAGE in a 15% polyacrylamide gel, at least 15 components with mol. wts 12,000-100,000 bound IgE from the panel of patient sera. A component of mol. wt 22,000 bound IgE from at least 94% of the patient sera tested and for all but three sera this component also bound the greatest quantity of IgE. Five other components with mol. wts 12,000, 17,000, 29,000, 39,000 and 42,000 bound IgE from 75-94% of the patient sera. After separation by IEF, at least 28 protein bands were detected in the pI region 3.5-7.2 and at least seven bands were found in the region 8.6-9.3. At least 11 bands in the pI range 4.2-7.3 and at least five bands in the pI region 8.5-9.2 bound IgE from the panel of patient sera. The most intense radiostaining was observed with a component having a pI of 4.35, which bound IgE from 31% of the patient sera. Immunoblotting of the SDS-PAGE and IEF gels using specific rabbit antisera and human sera against three important mugwort pollen allergens, denoted Ag 9, Ag 12 and Ag 13, was performed to determine the mol. wt and pI of these allergens which had earlier only been identified in CIE/CRIE. The results revealed that Ag 13 had a mol. wt of 61,000 and a pI of 4.35, Ag 12 had a mol. wt of 22,000 and AG 9 had pIs in the region 4.55-5.55 (six isoforms). Ag 9 did not bind IgE after SDS-PAGE and was thus not identified in the SDS-PAGE pattern, and Ag 12 failed to be detected in the NCM after transfer from IEF gels. By crossed immunoelectrofocusing, Ag 12 was found to consist of several isoforms predominantly located in the pI region 3.5-5.1. The immunoblotting analysis also revealed that the glycoprotein allergen Art v II was not detected after transfer from either SDS-PAGE or IEF gels. In conclusion, immunoblotting analysis of SDS-PAGE and IEF gels are useful methods for characterization of mugwort pollen extract, but it should be noted that some important allergens which are easily identified in CIE/CRIE may fail to be detected by these methods.
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PMID:Identification and characterization of important allergens from mugwort pollen by IEF, SDS-PAGE and immunoblotting. 185 51


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