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Academic literature on the topic 'Crosslinking (Polymerization) Gel electrophoresis'

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Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Huh, MM, BP Schick, PK Schick, and RW Colman. "Covalent crosslinking of human coagulation factor V by activated factor XIII from guinea pig megakaryocytes and human plasma." Blood 71, no. 6 (June 1, 1988): 1693–702. http://dx.doi.org/10.1182/blood.v71.6.1693.1693.

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Abstract Coagulation factor V (FV) has been shown to be synthesized in both the liver and megakaryocytes. We now present evidence that FV can be covalently crosslinked by an enzyme originating from megakaryocytes to form polymeric multimers of factor V. The guinea pig megakaryocyte enzyme appears to be factor XIIIa since the FV-crosslinking activity (1) had an absolute requirement for Ca++, (2) was completely inhibited by iodoacetamide, 5,5′-dithiobis- (2-nitrobenzoic acid), p- chloromercuribenzene sulfonic acid, and N-ethylmaleimide, all known alkylators of the thiol group at the active site of the factor XIIIa, (3) was blocked by known pseudoamine donor substrates of factor XIIIa including dansylcadaverine and putrescine, and (4) could be directly demonstrated in the guinea pig megakaryocyte lysate by a specific activity staining procedure. No tranglutaminase was detected in guinea pig megakaryocytes in contrast to red cells and liver. A similar pattern of covalent crosslinking of human FV by purified activated human plasma factor XIII was also demonstrated. Analysis of the crosslinked products of FV formed by the guinea pig enzyme by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicates the formation of intermediate as well as higher molecular weight polymers, suggesting that the crosslinking is a stepwise polymerization process.

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Coagulation factor V (FV) has been shown to be synthesized in both the liver and megakaryocytes. We now present evidence that FV can be covalently crosslinked by an enzyme originating from megakaryocytes to form polymeric multimers of factor V. The guinea pig megakaryocyte enzyme appears to be factor XIIIa since the FV-crosslinking activity (1) had an absolute requirement for Ca++, (2) was completely inhibited by iodoacetamide, 5,5′-dithiobis- (2-nitrobenzoic acid), p- chloromercuribenzene sulfonic acid, and N-ethylmaleimide, all known alkylators of the thiol group at the active site of the factor XIIIa, (3) was blocked by known pseudoamine donor substrates of factor XIIIa including dansylcadaverine and putrescine, and (4) could be directly demonstrated in the guinea pig megakaryocyte lysate by a specific activity staining procedure. No tranglutaminase was detected in guinea pig megakaryocytes in contrast to red cells and liver. A similar pattern of covalent crosslinking of human FV by purified activated human plasma factor XIII was also demonstrated. Analysis of the crosslinked products of FV formed by the guinea pig enzyme by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicates the formation of intermediate as well as higher molecular weight polymers, suggesting that the crosslinking is a stepwise polymerization process.

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Naryzhny, Stanislav N., Leroi V. DeSouza, K. W. Michael Siu, and Hoyun Lee. "Characterization of the human proliferating cell nuclear antigen physico-chemical properties: aspects of double trimer stability." Biochemistry and Cell Biology 84, no. 5 (October 2006): 669–76. http://dx.doi.org/10.1139/o06-037.

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Its toroidal structure allows the proliferating cell nuclear antigen (PCNA) to wrap around and move along the DNA fiber, thereby dramatically increasing the processivity of DNA polymerization. PCNA is also involved in the regulation of a wide spectrum of other biological functions, including epigenetic inheritance. We have recently reported that mammalian PCNA forms a double trimer complex, which may be critically important in coordinating DNA replication and other cellular functions. To gain a better understanding of the stability of PCNA complexes, we characterized the physico-chemical properties of the PCNA structure by in vivo and in vitro approaches. The data obtained by gel filtration and nondenaturing gel electrophoresis of native PCNA molecules confirm our previous observations, obtained using formaldehyde crosslinking, in which PCNA exists in the cell as a double trimer. We have also found that optimal pH (pH 6.5–7.5) is critical for the stability of the PCNA structure. The presence or absence of ATP, dithiothreitol, and Mg2+ does not affect the stability of the PCNA trimer or double trimer. However, 0.02% SDS can effectively inhibit PCNA double trimer, but not single trimer, formation. Interestingly, glycerol and ammonium sulfate significantly destabilize both PCNA trimer and double trimer structures.

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Yoshida, Nobuhiko, Shingi Imaoka, Hajime Hirata, Michio Matsuda, and Shinji Asakura. "Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant." Thrombosis and Haemostasis 68, no. 05 (1992): 534–38. http://dx.doi.org/10.1055/s-0038-1646313.

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SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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Yoshida, N., M. Okuma, M. Moroi, and M. Matsuda. "A lower molecular weight gamma-chain variant in a congenital abnormal fibrinogen (Kyoto)." Blood 68, no. 3 (September 1, 1986): 703–7. http://dx.doi.org/10.1182/blood.v68.3.703.703.

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Abstract A gamma-chain variant with a lower molecular weight than the normal gamma chain was detected in a new congenital abnormal fibrinogen with impaired polymerization of the fibrin monomer and with normal release of fibrinopeptides A and B in a 45-year-old male. Purified fibrinogen analyzed on SDS-polyacrylamide gel electrophoresis under the reduced condition contained an abnormal protein band with an apparent molecular weight of 48,000 compared with the gamma chain with a molecular weight of 50,000. This abnormal protein band was found to be a gamma-chain variant from the molar ratio of A alpha chain:B beta chain:gamma chain:abnormal protein (about 2:2:1:1), with positive staining for carbohydrate and crosslinking ability. Crosslinked fibrin contained three types of gamma-gamma dimers with apparent molecular weights of 94,000 (the same as normal major gamma-gamma dimer), 92,000 and 90,000, and the plasmic digests of crosslinked fibrin in the presence of calcium retained three types of gamma-gamma dimer remnants. This suggests that the abnormal gamma-chain variant has a shorter polypeptide chain not in the NH2-terminal but in the COOH-terminal portion, probably at or near the polymerization site. This patient's two daughters had the same abnormal fibrinogen. This unique inherited abnormal fibrinogen was designated as fibrinogen Kyoto, and the gamma- chain variant as gamma Kyoto.

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A gamma-chain variant with a lower molecular weight than the normal gamma chain was detected in a new congenital abnormal fibrinogen with impaired polymerization of the fibrin monomer and with normal release of fibrinopeptides A and B in a 45-year-old male. Purified fibrinogen analyzed on SDS-polyacrylamide gel electrophoresis under the reduced condition contained an abnormal protein band with an apparent molecular weight of 48,000 compared with the gamma chain with a molecular weight of 50,000. This abnormal protein band was found to be a gamma-chain variant from the molar ratio of A alpha chain:B beta chain:gamma chain:abnormal protein (about 2:2:1:1), with positive staining for carbohydrate and crosslinking ability. Crosslinked fibrin contained three types of gamma-gamma dimers with apparent molecular weights of 94,000 (the same as normal major gamma-gamma dimer), 92,000 and 90,000, and the plasmic digests of crosslinked fibrin in the presence of calcium retained three types of gamma-gamma dimer remnants. This suggests that the abnormal gamma-chain variant has a shorter polypeptide chain not in the NH2-terminal but in the COOH-terminal portion, probably at or near the polymerization site. This patient's two daughters had the same abnormal fibrinogen. This unique inherited abnormal fibrinogen was designated as fibrinogen Kyoto, and the gamma- chain variant as gamma Kyoto.

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Yoshida, N., K. Ota, M. Moroi, and M. Matsuda. "An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine." Blood 71, no. 2 (February 1, 1988): 480–87. http://dx.doi.org/10.1182/blood.v71.2.480.480.

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Abstract A gamma-chain variant with an apparently higher molecular weight than the normal gamma-chain was detected in a new congenital abnormal fibrinogen with impaired polymerization of the fibrin monomer and with normal release of fibrinopeptides A and B in a 51-year-old male. Purified fibrinogen analyzed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under the reduced condition in the system of Laemmli contained two protein bands in the gamma-chain region (molecular weight, 50,500 as compared with 50,000 for the normal), both with normal crosslinking ability. The presence of two types of gamma- chains was more clearly detected when reduced and carboxymethylated fibrinogen was analyzed by SDS-PAGE or when reduced fragment D2 was analyzed on SDS-PAGE followed by Western blotting, and identified by positive staining for anti gamma-chain monoclonal antibody. Cyanogen bromide- or lysylendopeptidase-cleavage of purified gamma-chains analyzed on reverse-phase high performance liquid chromatography showed the decrease of one peptide compared with the normal and the appearance of an abnormal peptide peak. Amino acid sequence analysis demonstrated that the gamma arginine-275 of gamma-chain variant was replaced by a cysteine. These data suggest that some regions or conformations containing gamma 275 will affect the polymerization of fibrin monomers. The propositus' two daughters had the same abnormal fibrinogen. This unique inherited abnormal fibrinogen was designated as fibrinogen Tochigi, and the gamma-chain variant as gamma Tochigi.

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Abstract:

A gamma-chain variant with an apparently higher molecular weight than the normal gamma-chain was detected in a new congenital abnormal fibrinogen with impaired polymerization of the fibrin monomer and with normal release of fibrinopeptides A and B in a 51-year-old male. Purified fibrinogen analyzed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under the reduced condition in the system of Laemmli contained two protein bands in the gamma-chain region (molecular weight, 50,500 as compared with 50,000 for the normal), both with normal crosslinking ability. The presence of two types of gamma- chains was more clearly detected when reduced and carboxymethylated fibrinogen was analyzed by SDS-PAGE or when reduced fragment D2 was analyzed on SDS-PAGE followed by Western blotting, and identified by positive staining for anti gamma-chain monoclonal antibody. Cyanogen bromide- or lysylendopeptidase-cleavage of purified gamma-chains analyzed on reverse-phase high performance liquid chromatography showed the decrease of one peptide compared with the normal and the appearance of an abnormal peptide peak. Amino acid sequence analysis demonstrated that the gamma arginine-275 of gamma-chain variant was replaced by a cysteine. These data suggest that some regions or conformations containing gamma 275 will affect the polymerization of fibrin monomers. The propositus' two daughters had the same abnormal fibrinogen. This unique inherited abnormal fibrinogen was designated as fibrinogen Tochigi, and the gamma-chain variant as gamma Tochigi.

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Quarless, Shelley A., and Charles R. Cantor. "Analysis of RNA structure by ultraviolet crosslinking and denaturation gel electrophoresis." Analytical Biochemistry 147, no. 2 (June 1985): 296–300. http://dx.doi.org/10.1016/0003-2697(85)90275-1.

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Ida, Shohei, Akimitsu Katsurada, Mitsuhiro Tsujio, Motoharu Nakamura, and Yoshitsugu Hirokawa. "Crosslinker-Based Regulation of Swelling Behavior of Poly(N-isopropylacrylamide) Gels in a Post-Polymerization Crosslinking System." Gels 6, no. 1 (December 21, 2019): 2. http://dx.doi.org/10.3390/gels6010002.

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A fundamental understanding of the effect of a crosslinker on gel properties is important for the design of novel soft materials because a crosslinking is a key component of polymer gels. We focused on post-polymerization crosslinking (PPC) system utilizing activated ester chemistry, which is a powerful tool due to structural diversity of diamine crosslinkers and less susceptibility to solvent effect compared to conventional divinyl crosslinking system, to systematically evaluate the crosslinker effect on the gel properties. A variety of alkyldiamine crosslinkers was employed for the synthesis of poly(N-isopropylacrylamide) (PNIPAAm) gels and it was clarified that the length of alkyl chains of diamine crosslinkers strongly affected the gelation reaction and the swelling behavior. The longer crosslinker induced faster gelation and decreased the swelling degree and the response temperature in water, while the crosslinking density did not significantly change. In addition, we were able to modify the polymer chains in parallel with crosslinking by using a monoamine modifier along with a diamine crosslinker. This simultaneous chain modification during crosslinking (SMC) was demonstrated to be useful for the regulation of the crosslinking density and the swelling behavior of PNIPAAm gels.

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Dissertations / Theses on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Wang, Luxin Fan Xudong Mustapha Azlin. "Applications of gel electrophoresis in quantum dot conjugates' separation and purification." Diss., Columbia, Mo. : University of Missouri--Columbia, 2009. http://hdl.handle.net/10355/6486.

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Title from PDF of title page (University of Missouri--Columbia, viewed on Feb 19, 2010). The entire thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file; a non-technical public abstract appears in the public.pdf file. Thesis advisor: Dr. Xudong Fan and Dr. Azlin Mustapha. Includes bibliographical references.

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Litt, Lloyd C. "An investigation of electrophoresis gel silver staining using large area sample inclusive polymerization /." Online version of thesis, 1989. http://hdl.handle.net/1850/11463.

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Gerard, Eric-Jack. "Synthese, caracterisation et comportement de polyurethannes hydrophiles : etude du mecanisme de la polycondensation reticulante." Université Louis Pasteur (Strasbourg) (1971-2008), 1988. http://www.theses.fr/1988STR13192.

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Synthese d'hygrogels, constitues de chaines elastiques de polydioxolanne. Les reticulats sont synthetises en milieu organique par couplages multiples des extremites hydroxylees, du polydioxolanne precurseur avec un compose isocyanate plurifonctionnel. Apres reaction, un echange progressif du solvant organique par l'eau permet d'obtenir les hydrogels

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Book chapters on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Spanswick, Victoria J., Janet M. Hartley, and John A. Hartley. "Measurement of DNA Interstrand Crosslinking in Individual Cells Using the Single Cell Gel Electrophoresis (Comet) Assay." In Methods in Molecular Biology, 267–82. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-418-0_17.

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Conference papers on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Francis, C. W., and V. J. Marder. "RAPID FORMATION OF LARGE MOLECULAR WEIGHT O-P0LYMERS IN CROSSLINKED FIBRIN INDUCED BY HIGH FACTOR XIII CONCENTRATIONS: ROLE OF PLATELET FACTOR XIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643311.

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Following fibrin polymerization, activated factor XIII stabilizes the clot by catalyzing the formation of specific intermolecular covalent crosslinks between pairs of y chains to form dimers and also among two or more a chains to form polymers. We have identified a series of previously uncharacterized a chain polymers with a wide range of sizes, including some with apparent Mr in excess of several million. Additionally, we establish the role of high concentrations of factor XIII in the extent and rate of α-polymer formation and provide evidence that the factor XIII required can be provided by platelets. Using SDS gel electrophoresis, we find that fibrin prepared from purified fibrinogen or from platelet-deficient plasma contains a series of 21 factor XIIIa crosslinked a chain polymers with Mr from 140,000 to 770,000. The mean Mr difference between individual polymers of 32,000 is consistent with a staggered, overlapping sequential addition of monomers to the growing α-polymer chain. In plasma containing no platelets, α-polymer formation was incomplete with residual α-monomer remaining. Progressively higher platelet counts facilitated more rapid crosslinking of a chains into larger polymers. Intact platelets were not required to promote crosslinking, since platelets lysed by freezing and thawing were also effective. Enrichment of plasma with placental factor XIII in an amount equal to that contained in platelets was as effective as platelets in accelerating the rate of formation and increasing the size of α-chain polymers. We conclude that platelets are a principal source of factor XIII for maximal fibrin stabilization, providing a larger quantity than is available from plasma alone and regulating both the rate and extent of α-polymer formation in thrombi or hemostatic plugs at sites of vascular injury.

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Kaminski, M., and J. McDonagh. "CALCIUM-INDUCED FORMATION OF FIBRINOGEN -- FIBRIN COMPLEXES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643331.

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Presence of calcium chloride (8.3 mM) at u = 0.1 enhanced precipitate formation in several different fibrinogen preparations. The precipitate had gel like properties and demonstrated syneresls when disturbed. Precipitation proceeded in the time dependent manner with a plateau after 30 min. The amount of precipitate ranged from 4-24% of total protein content of different preparations. Precipitates did form at u = 0.1 without calcium ion; however, the amount of protein was 3 to 7 fold less than when calcium ion was present.SOS gel electrophoresis of calcium precipitates demonstrated cross-linking of gamma chains. Cross-linking, but not precipitate formation was blocked by parachloromercurie-benzoate (PCMB). The precipitates were redissolved in 2M urea, treated with thrombin, and analyzed for flbrinopeptide content by HLPC. Precipitate formed in absence of calcium ion contained 19% of FPA and 89% of FPB. Precipitates formed in the presence of calcium ion contained 49% of the expected amount of FPA and 98% of expected FPB. The precipitation phenomenon could be reproduced after fibrin monomer-free fibrinogen (prepared by dialysis of calcium supernatants against calcium free buffer) was treated briefly with thrombin.The above finding suggests that calcium ion enhances polymerization of Intact fibrinogen and molecules missing one or two FPA's.

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Kuyas, C., A. Haeberli, and P. W. Straub. "SEPARATION OF FIBRINOGEN FRAGMENTS ON GLYPRQARGPROLYS-FRACTOGEL." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642885.

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The tetrapeptide GlyProArgPro, which corresponds to the newly exposed N-terminal sequence of fibrin a-polypeptide chain after the action of thraribin, has a binding site in the C-terminal part of the ;-chain as suggested by several authors. Using Gly-ProArgProLys-Fractogel (GPRPK) chrcmatography we tried to isolate a fibrinogen fragment, obtained with different enzymes and conditions, which includes the binding site for GPRP. Human fibrinogen was digested by plasmin in presence and absence of Ca-ions, and the resulting lysates were applied in 0.05 M triethanolamine (TEA), 0.1 M NaCl pH 7.4 to the GPRPK-Fractogel. The gel was washed extensively with TEA-buffer and the adsorbed protein was eluted with 6M urea in TEA-buffer. The protein containing fractions were analyzed iiununologically with anti-fragment E- and with anti-fragment D antibodies. Human fibrinogen was also digested with endopeptidase Arg-C in O.IM NaHco3 pH 8.0 at 37C over night. The enzyme cleaves fibrinogen to fragments, one of which comprising the y-chain sequence 275-375 which is said to contain the fibrin polymerization site. The Arg C-lysate was chromatographed on GPRPK-Fractogel. All fragments were analyzed by SDS-electrophoresis and by reversed-phase HPLC.Fragment D1 was the only fibrinogen fragment which was adsorbed on GPRPK-Fractogel. All other assayed fibrinogen fragments obtained by enzymatic cleavage, showed no affinity to GPRPK-Fractogel. These results demonstrate that for the binding of GPRP to fibrinogen a conformationally intact γ-chain remnant of the fragment D is required.One step chrcmatography using GPRPK-Fractogel can thus also be used to isolate fragment D1 in high purity fran plasmin lysates of fibrinogen.

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Academic literature on the topic 'Crosslinking (Polymerization) Gel electrophoresis'

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Journal articles on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Dissertations / Theses on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Book chapters on the topic "Crosslinking (Polymerization) Gel electrophoresis"

Conference papers on the topic "Crosslinking (Polymerization) Gel electrophoresis"