Heterogeneity of lipoprotein Lp(a) and apolipoprotein(a).

1988 ◽  
Vol 34 (6) ◽  
pp. 1036-1040 ◽  
Author(s):  
G F Grinstead ◽  
R D Ellefson
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Core Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Single Patient ◽  
Selective Precipitation ◽  
Apolipoprotein A ◽  
Molecular Masses ◽  
Chemical Deglycosylation

Abstract We have purified Lp(a) lipoproteins from sera of four subjects by ultracentrifugation, selective precipitation, and chromatofocusing. Each subject had two forms of serum Lp(a) that were separable by chromatofocusing. We purified apolipoprotein (a) [apo(a)] from the eight isolated Lp(a)s and obtained only one form of apo(a) from each subject. The four apo(a)s seen on sodium dodecyl sulfate-polyacrylamide gel electrophoresis had different apparent molecular masses, ranging from 275 to 440 kDa. Chemical deglycosylation of the smallest apo(a) yielded a 235 kDa protein, which may be a core protein structure common to all apo(a)s. We conclude that there are many forms of serum Lp(a) and apo(a). The heterogeneity of serum Lp(a) particles can be ascribed in part to differences in size of apo(a), but other factors must account for the existence within a single patient of different Lp(a)s that contain apparently identical apo(a). One must consider the heterogeneity of Lp(a) when designing assays for this lipoprotein.

Analysis for Cerebrospinal Fluid Proteins by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

1992 ◽  
Vol 38 (10) ◽  
pp. 2008-2012 ◽  
Author(s):  
F Mashige ◽  
T Shimizu ◽  
S Iijima ◽  
A Ohkubo
Keyword(s):  
Cerebrospinal Fluid ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Apolipoprotein A ◽  
Csf Proteins ◽  
Sds Page ◽  
Molecular Masses

Abstract Cerebrospinal fluid (CSF) proteins with molecular masses of < 150,000 Da were identified by immunoblotting after two kinds of nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). With PAGE 1 (17-27% gradient gel), CSF proteins were clearly separated into seven to nine bands with molecular masses of 3000-67,000 Da; seven bands were identified as beta 2-microglobulin, lysozyme, prealbumin, free kappa and lambda chain, apolipoprotein A-I, glycoproteins, and albumin by immunoblotting. With PAGE 2 (10-20% gradient gel), proteins were clearly separated into 11-16 bands with molecular masses of 15,000-150,000 Da; 11 were identified as prealbumin, free kappa and lambda chain, apolipoprotein A-I, glycoproteins, albumin, alpha 1-antitrypsin, transferrin (separated into two bands), immunoglobulin fragments, haptoglobin, and IgG. We analyzed CSF samples collected from 81 patients with cerebrospinal signs by these SDS-PAGE methods and observed prominent bands in some cases.

scholarly journals Differential Transmission of Isolates of the High Plains virus by Different Sources of Wheat Curl Mites

Plant Disease ◽  
2002 ◽  
Vol 86 (2) ◽  
pp. 138-142 ◽  
Author(s):  
Dallas L. Seifers ◽  
Tom L. Harvey ◽  
Raymond Louie ◽  
D. T. Gordon ◽  
T. J. Martin
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
South Dakota ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
High Plains ◽  
Aceria Tosichella ◽  
Molecular Masses ◽  
Differential Transmission ◽  
Different Sources

High Plains virus (HPV) isolates from Colorado, Idaho, Kansas, Texas, and Utah were serologically related, had similar relative molecular masses (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) for the 32-kDa diagnostic HPV protein, and were transmissible and maintained free of Wheat streak mosaic virus (WSMV) by vascular puncture inoculation. Collections of wheat curl mites (Aceria tosichella Keifer; WCM) from Kansas, Montana, Nebraska, South Dakota, and Texas differentially transmitted these isolates. For collections from South Dakota and Texas, little or no HPV transmission occurred, whereas WCM from Nebraska and Montana transmitted all five isolates. The collection from Kansas mostly transmitted only one HPV isolate. Aviruliferous or viruliferous WSMV Nebraska WCM transmitted HPV at similar rates and aviruliferous Montana WCM transmitted HPV at lower levels than viruliferous Montana WCM.

Purification and Properties of Two Thermostable Alkaline Xylanases from an Alkaliphilic Bacillussp

1998 ◽  
Vol 64 (9) ◽  
pp. 3533-3535 ◽  
Author(s):  
Amare Gessesse
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Good Stability ◽  
Purification And Properties ◽  
Molecular Masses ◽  
Ph Range ◽  
Temperature Optima

ABSTRACT Two xylanases, designated XylA and XylB, were purified from the culture supernatant of the alkaliphilic Bacillus sp. strain AR-009. The molecular masses of the two enzymes were estimated to be 23 kDa (XylA) and 48 kDa (XylB) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pHs for activity were 9 for XylA and 9 to 10 for XylB. The temperature optima for the activity of XylA were 60°C at pH 9 and 70°C at pH 8. XylB was optimally active at 75°C at pH 9 and 70°C at pH 8. Both enzymes were stable in a broad pH range and showed good stability when incubated at 60 and 65°C in pH 8 and 9 buffers.

scholarly journals Biochemical and Genetic Characterization oftrans-2′-Carboxybenzalpyruvate Hydratase-Aldolase from a Phenanthrene-Degrading Nocardioides Strain

1998 ◽  
Vol 180 (4) ◽  
pp. 945-949 ◽  
Author(s):  
Tokuro Iwabuchi ◽  
Shigeaki Harayama
Keyword(s):  
Amino Acid ◽  
Sodium Dodecyl Sulfate ◽  
Amino Acid Sequence ◽  
Gel Electrophoresis ◽  
Genetic Characterization ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Degrading Bacterium ◽  
Molecular Masses

ABSTRACT trans-2′-Carboxybenzalpyruvate hydratase-aldolase was purified from a phenanthrene-degrading bacterium,Nocardioides sp. strain KP7, and characterized. The purified enzyme was found to have molecular masses of 38 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 113 kDa by gel filtration chromatography. Thus, the homotrimer of the 38-kDa subunit constituted an active enzyme. The Km andkcat values of this enzyme fortrans-2′-carboxybenzalpyruvate were 50 μM and 13 s−1, respectively.trans-2′-Carboxybenzalpyruvate was transformed to 2-carboxybenzaldehyde and pyruvate by the action of this enzyme. The structural gene for this enzyme was cloned and sequenced; the length of this gene was 996 bp. The deduced amino acid sequence of this enzyme exhibited homology to those oftrans-2′-hydroxybenzalpyruvate hydratase-aldolases fromPseudomonas putida PpG7 and Pseudomonas sp. strain C18.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

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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