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Jankova, L.
Stanford Linear Accelerator Center, Menlo Park, CA (United States); Stanford Synchrotron Radiation Lab. (United States). Funding organisation: USDOE Office of Science (United States)2001
Stanford Linear Accelerator Center, Menlo Park, CA (United States); Stanford Synchrotron Radiation Lab. (United States). Funding organisation: USDOE Office of Science (United States)2001
AbstractAbstract
No abstract available
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Source
SLAC-REPRINT--2001-173; AC03-76SF00515
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Journal Article
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Journal of Biological Chemistry; ISSN 0021-9258;
; (1Jan2001issue); [10 p.]

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[en] A method for calculating small-angle scattering profiles using Monte Carlo simulation of the scattering volume is described. From the simulated volume the distance distribution function is calculated directly and a simple Fourier transformation produces the scattering profile. The method is easy to apply to molecules of any shape and composition. Here it is tested against the theoretical profile for a sphere and for an ellipsoid. Finally, the method is applied to a scatterer composed of three spheres connected by a long rod (a model for the biomolecule fibrinogen). (orig.)
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[en] The proton resonances of the following synthetic linear human fibrinogen-like peptides were completely assigned with two-dimensional NMR techniques in solution: Ala(1)-Asp-Ser-Gly-Glu-Gly-Asp(7)-Phe-Leu-Ala-Glu-Gly(12)-Gly(13)-Gly(14)-Val(15)-Arg(16)-Gly-Pro-Arg-Val-Val-Glu-Arg (F10), Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly(13)-Gly(14)-Val-Arg (F11), and Gly-Pro-Arg-Val-Val-Glu-Arg (F12). No predominant structure was found in the chain segment from Ala(1) to Gly (6) for F10 in both H2O and dimethyl sulfoxide. The previous suggestion that there is a hairpin loop involving residues Gly(12) to Val(15) in the Aα chain of human fibrinogen is supported by the slow backbone NH exchange rates of Gly(14) and Val(15), by an unusually small NH chemical shift of Val(15), and by strong sequential NOE's involving this region in F10. This local chain fold within residues Asp(7) to Val(20) may place the distant Phe residue near the Arg(16)-Gly(17) peptide bond which is cleaved by thrombin
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Olexa, S.A.; Knight, L.C.; Budzynski, A.Z.
Temple Univ., Philadelphia, PA (United States)1989
Temple Univ., Philadelphia, PA (United States)1989
AbstractAbstract
[en] The patent deals with a method of locating thrombi in vivo, comprising the steps of administering a radiolabelled peptide selected from the group consisting of Fragment E1 isolated from cross-linked fibrin, Fragment E2 isolated from cross-linked fibrin, and peptides having an amino acid sequence intermediate between Fragments E1, and E2 derived from cross-linked fibrin by plasmin digestion to a human or animal wherein the peptide, is selectively incorporated or bound by forming a preformed thrombi and externally detecting the radiation emitted by the radiolabelled peptide. A composition containing the peptide used for locating thrombi is also disclosed. 6 tabs
Original Title
Blanding for bruk ved ekstern paavisning og lokalisering av blodpropp
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Source
15 Mar 1989; 2 Apr 1981; 22 p; NO PATENT DOCUMENT 160114/C/; US PRIORITY 250174; Priority date: 2 Apr 1981
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Patent
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AbstractAbstract
[en] Short communications only
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Source
Wu Jilan; Takehisa, M; 368 p; 1992; p. 181; 8. international meeting on radiation processing; Beijing (China); 13-18 Sep 1992; Available from China Nuclear Information Centre
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Miscellaneous
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[en] Apolipoprotein(a) [apo(a)] is a glycoprotein with M/sub r/ ∼ 280,000 that is disulfide linked to apolipoprotein B in lipoprotein(a) particles. Elevated plasma levels of lipoprotein(a) are correlated with atherosclerosis. Partial amino acid sequence of apo(a) shows that it has striking homology to plasminogen. Plasminogen is a plasma serine protease zymogen that consists of five homologous and tandemly repeated domains called kringles and a trypsin-like protease domain. The amino-terminal sequence obtained for apo(a) is homologous to the beginning of kringle 4 but not the amino terminus of plasminogen. Apo(a) was subjected to limited proteolysis by trypsin or V8 protease, and fragments generated were isolated and sequenced. Sequences obtained from several of these fragments are highly (77-100%) homologous to plasminogen residues 391-421, which reside within kringle 4. Analysis of these internal apo(a) sequences revealed that apo(a) may contain at least two kringle 4-like domains. A sequence obtained from another tryptic fragment also shows homology to the end of kringle 4 and the beginning of kringle 5. Sequence data obtained from the two tryptic fragments shows homology with the protease domain of plasminogen. One of these sequences is homologous to the sequences surrounding the activation site of plasminogen. Plasminogen is activated by the cleavage of a specific arginine residue by urokinase and tissue plasminogen activator; however, the corresponding site in apo(a) is a serine that would not be cleaved by tissue plasminogen activator or urokinase. Using a plasmin-specific assay, no proteolytic activity could be demonstrated for lipoprotein(a) particles. These results suggest that apo(a) contains kringle-like domains and an inactive protease domain
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Journal Article
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Proceedings of the National Academy of Sciences of the United States of America; ISSN 0027-8424;
; CODEN PNASA; v. 84(10); p. 3224-3228

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Wang, H.; Yokota, H.; Kim, R.; Kim, S.-H.
Ernest Orlando Lawrence Berkeley National Lab., Advanced Light Source, Berkeley, CA (United States). Funding organisation: US Department of Energy (United States)1999
Ernest Orlando Lawrence Berkeley National Lab., Advanced Light Source, Berkeley, CA (United States). Funding organisation: US Department of Energy (United States)1999
AbstractAbstract
No abstract available
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Source
LBNL/ALS--13043; AC03-76SF00098; Journal Publication Date: January 1999
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Journal Article
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Acta Crystallographica. Section D: Biological Crystallography; ISSN 0907-4449;
; v. 55(PT.1); [10 p.]

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AbstractAbstract
[en] It became apparent in 1978 that some radioassays for Vitamin B-12 were falsely normal. This investigation was performed to assure the accuracy of our assay. False normal B-12 levels may result in permanent damage or delay in relieving distressful symptoms. False low levels result in no permanent sequalae. ''Normal'' values should be set with these consequences in mind. The authors reviewed clinical charts on patients with <300 pg/m1 serum B-12 in 1000 consecutive determinations and all patients newly diagnosed B-12 deficient 1/1/83 to 10/14/83. Simu1TRAC Radioassay, Becton Dickinson Co., modified by correction for serum nonspecific binding is used. ''Normal'' values (234-1000 pg/m1) are based on 47 outpatients. 176 of the 1000 assays resulted in levels <300 pg/m1. 87 were from other location with no clinical information. 89 assays on Marshfield Clinic patients included 2 duplicates. 45 patients were newly diagnosed B-12 deficient 1/1/83 to 10/14/83. 12 were diagnosed elsewhere and on therapy. 32 had assays <234 pg/m1. 1 with normal B-12 is ''possibly deficient'', a Schilling test is scheduled. The authors conclude that their B-12 assay has correctly identified 32 clinically accepted B-12 deficient patients. 1 possibly deficient patient was normal. 25 of 42 patients with levels below normal are deficient. The false positive rate is felt acceptable in view of the false negative rate and the consequences of the respective errors
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Source
31. annual meeting of the Society of Nuclear Medicine; Los Angeles, CA (USA); 5-8 Jun 1984; CONF-840619--
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[en] The identification of structural markers for B12/protein interactions is crucial to a complete understanding of vitamin B12 transport and metabolic reaction mechanisms of B12 coenzymes. Fourier transform infrared spectroscopy can provide direct measurements of changes in the side chains and corrin ring resulting from B12/protein interactions. Using FTIR spectroscopy in various solvent systems, the authors have identified structural markers for corrinoids in the physiological state. They assign the major band (denoted B), which occurs at ca. 1,630 cm-1 in D2O and ca. 1675 cm-1 in ethanol, to the amide I C double-bond stretching mode of the propionamide side chains of the corrin ring. The lower frequency of band B in D2O versus ethanol is due to the greater hydrogen-bonding properties of D2O that stabilize the charged amide resonance form. Since the propionamides are known to be important in protein binding, band B is a suitable marker for monitoring the interaction of these side chains with proteins. They assign bands at ca. 1,575 and 1,545 cm-1 (denoted C and D) as breathing modes of the corrin ring on the basis of the bands' solvent independence and their sensitivity to changes in axial ligation
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Noto, M.G.; Rabiller, Graciela; Garrie Faget, Claudio; Fisman, Carlos; Manzini, Alberto
Progress in radiopharmacology1987
Progress in radiopharmacology1987
AbstractAbstract
[en] A method of fibrinogen preparation is presented in order to label it with 99mTc employing Sn as reducing agent in alkaline medium. Purity controls by chromatography, coagulation in rabbits and biodistribution in rats were performed. It is concluded that optimal time incubation is between 22 and 23 hs. (M.E.L.)
[es]
Se presenta un metodo de preparacion de fibrinogeno para marcar con 99mTc utilizando como reductor Sn en medio alcalino. Los controles de pureza se efectuaron por cromatografia, los de coagulabilidad con sangre de conejo y la biodistribucion en ratones. Se concluye que el tiempo optimo de incubacion esta entre 22 y 23 h. (M.E.L.)Original Title
Preparacion y control de calidad de fibrinogeno 99mTc
Secondary Subject
Source
Mitta, A.E.A.; Canellas, C.O. (Comision Nacional de Energia Atomica, Buenos Aires (Argentina)); Caro, R.A. (Buenos Aires Univ. (Argentina). Facultad de Farmacia y Bioquimica) (eds.); Comision Nacional de Energia Atomica, Buenos Aires (Argentina); 212 p; 1987; p. 202-206; 5. International symposium on radiopharmacology; Buenos Aires (Argentina); 29-31 Oct 1986
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Miscellaneous
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