Studies on the Stellaria longipes complex (Caryophyllaceae). VII. The seed proteins

1986 ◽  
Vol 64 (7) ◽  
pp. 1327-1330 ◽  
Author(s):  
David J. Gifford ◽  
C. C. Chinnappa
Keyword(s):  
Species Complex ◽  
Polyacrylamide Gel Electrophoresis ◽  
General Pattern ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Distinct Species ◽  
Major Protein ◽  
Stellaria Longipes ◽  
Cytogenetic Studies ◽  
Protein Components

Seed proteins of Stellaria longipes s.l. 2n = 52, 78, and 104, have been characterized using sodium dodecyl sulphate – polyacrylamide gel electrophoresis. The same general pattern as regards the number of major protein components resolved was observed in all the genotypes and cytotypes studied. These included all the morphotypes that were described as distinct species. The present data do not contradict the conclusions drawn from cytogenetic studies that all the morphological types are closely related and are part of a polyploid species complex.

Membranes of chromaffin granules. Isolation and partial characterization of two proteins

1971 ◽  
Vol 122 (3) ◽  
pp. 298.1-304 ◽  
Author(s):  
Heide Hörtnagl ◽  
H. Winkler ◽  
J. A. L. Schöpf ◽  
W. Hohenwallner
Keyword(s):  
Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Major Protein ◽  
Chromaffin Granules ◽  
Protein Components ◽  
Acid Gel ◽  
Total Membrane

Membranes of chromaffin granules were isolated from the adrenal glands of four different species. The solubilized membrane proteins could be resolved into several bands by polyacrylamide-gel electrophoresis (alkaline and acid gel systems). Two major protein components appeared to be common to the chromaffin granule membranes of ox, horse, pig and man. The various membrane proteins of bovine chromaffin granules were separated by filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. Two major membrane proteins (A and B) were obtained in purified form. Treatment of protein A with 2-mercaptoethanol before electrophoresis resulted in two more rapidly migrating subunits, whereas protein B was unaffected by mercaptoethanol treatment. The amino acid compositions of the two purified proteins were determined. They are very similar to that of the total membrane proteins but significantly different from that of the chromogranins, the soluble proteins of chromaffin granules.

Changes in the Polypeptide Composition of Maturing Seeds from Four Peanut (Arachis hypogaea L.) Cultivars1

1981 ◽  
Vol 8 (1) ◽  
pp. 6-10 ◽  
Author(s):  
Shaik-M. M. Basha ◽  
Sunil K. Pancholy
Keyword(s):  
Seed Development ◽  
Arachis Hypogaea ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Major Protein ◽  
Two Dimensional ◽  
Polypeptide Composition ◽  
Arachis Hypogaea L ◽  
Protein Components

Abstract Developing seeds from four peanut (Arachis hypogaea L.) cultivars were obtained and classified into Immature, Low-Intermediate, Intermediate, High-Intermediate and Mature groups. Seed proteins were extracted from the defatted meals using either 2 M NaCl, 0.01 M Tris HC1 (pH 8.2) or 9.3 M urea, 5 mM K2CO3, 2% Nonidet P-40 and 0.5% dithiothreitol and examined by one and two-dimensional polyacrylamide gel electrophoresis. Two dimensional gel electrophoresis showed major qualitative and quantitative changes in seed protein composition during maturation. Several major protein components gradually disappeared while others increased in their content. Major changes in the polypeptide composition were observed between the Intermediate and High-Intermediate maturity stages. In addition, the arachin (major storage globulin of peanut) components were present from the very early stages of seed development. Variation in the amount of protein components indicate selective synthesis and modification of certain seed proteins during seed development.

scholarly journals Identification and hemolytic activity of jellyfish (Rhopilema sp., Scyphozoa: Rhizostomeae) venom from the Persian Gulf and Oman Sea

2019 ◽  
Vol 20 (4) ◽  
pp. 1228-1232
Author(s):  
HOSSEIN JAFARI ◽  
HOSSEIN HONARI ◽  
JAMIL ZARGAN ◽  
SAEID TAMADONI JAHROMI
Keyword(s):  
Hemolytic Activity ◽  
Persian Gulf ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Biologically Active ◽  
Major Protein ◽  
Crude Venom ◽  
Oman Sea ◽  
Protein Components ◽  
The Persian Gulf

Abstract. Jafari H, Honari H, Zargan J, Jahromi ST. 2019. Identification and hemolytic activity of jellyfish (Rhopilema sp., Scyphozoa: Rhizostomeae) venom from the Persian Gulf and Oman Sea. Biodiversitas 20: 1228-1232. The present study investigated the hemolytic capacity of the crude venom extracted from isolated nematocysts of Rhopilema sp. Scyphozoa: Rhizostomeae. Nematocyst was used at various concentrations to evaluate the hemolytic activity by using the nematocysts of human, mice, and sheep. Mean concentration-dependent hemolysis could be observed from 200 µg/mL of protein equivalents or higher with variable potencies in different species. The crude venom was analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis SDS-PAGE. Molecular weight with 3 clear bands including 45, 65 and 95 kDa appeared to be the major protein components of the venom. The results of our experiments indicated that venom of Rhopilema sp. induces hemolysis in the studied species and determined that the increase in the amount of toxin has a positive correlation with the increase of cell lysis. This study showed that the venom of Rhopilema sp. may have many biologically active principles, which need further studies in the future.

A metalloproteinase extracellularly released byCrithidia deanei

2003 ◽  
Vol 49 (10) ◽  
pp. 625-632 ◽  
Author(s):  
Claudia Masini d'Avila-Levy ◽  
Rodrigo F Souza ◽  
Rosana C Gomes ◽  
Alane B Vermelho ◽  
Marta H Branquinha
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Residual Activity ◽  
Major Protein ◽  
Motile Cells ◽  
Sds Page ◽  
Triton X

Actively motile cells from a cured strain of Crithidia deanei released proteins in phosphate buffer (pH 7.4). The molecular mass of the released polypeptides, which included some proteinases, ranged from 19 to 116 kDa. One of the major protein bands was purified to homogeneity by a combination of anion-exchange and gel filtration chromatographs. The apparent molecular mass of this protein was estimated to be 62 kDa by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE). The incorporation of gelatin into SDS–PAGE showed that the purified protein presented proteolytic activity in a position corresponding to a molecular mass of 60 kDa. The enzyme was optimally active at 37 °C and pH 6.0 and showed 25% of residual activity at 28 °C for 30 min. The proteinase was inhibited by 1,10-phenanthroline and EDTA, showing that it belonged to the metalloproteinase class. A polyclonal antibody to the leishmanial gp63 reacted strongly with the released C. deanei protease. After Triton X-114 extraction, an enzyme similar to the purified metalloproteinase was detected in aqueous and detergent-rich phases. The detection of an extracellular metalloproteinase produced by C. deanei and some other Crithidia species suggests a potential role of this released enzyme in substrate degradation that may be relevant to the survival of trypanosomatids in the host.Key words: endosymbiont, trypanosomatid, extracellular, proteinase.

scholarly journals The 47-kD fragment of talin is a substrate for protein kinase P

Blood ◽  
1993 ◽  
Vol 82 (11) ◽  
pp. 3343-3349 ◽  
Author(s):  
PC Simons ◽  
L Elias
Keyword(s):  
Protein Kinase ◽  
Ion Exchange ◽  
Sequence Data ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Myelogenous Leukemia ◽  
Blue Staining ◽  
Major Protein

Abstract This laboratory has been characterizing protein serine/threonine kinase reactions of hematopoietic tissues, whose most distinguishing characteristics in vitro are stimulation with vesicular phosphatidyl glycerol, and the ability to function using Mn2+ as the sole divalent cation. The major protein substrates are a 73-kD protein and a protein migrating near ovalbumin on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The 47-kD protein was partially purified from cells harvested by leukapheresis from a patient with acute myelogenous leukemia, using ammonium sulfate precipitation and ion exchange chromatography. This partially purified ion-exchange fraction contained an endogenous kinase activity with characteristics similar to those we previously described of protein kinase P (protein kinase, phospholipid- stimulable: PK-P), but not typical of any form of protein kinase C (PK- C). With longer phosphorylation, the 47-kD band showed increasingly lower mobility demonstrable both by Coomassie blue staining and autoradiography, suggesting both that it was multiply phosphorylated, and that the excisable band was pure. The protein was thus eluted from preparative gel slices and digested with endoproteinase lys C. Sequence data from the fragments identified the protein as the 47-kD calpain fragment of talin, a protein found in focal adhesion plaques and some cell-cell contacts. PK-C phosphorylated the 47-kD protein, as has been reported previously, and phosphopeptide mapping disclosed a similar pattern of phosphorylation using either PK-C or the endogenous activity. The 47-kD protein labeled with the endogenous kinase contained predominantly phosphoserine, with some phosphothreonine and a trace of phosphotyrosine. Intact, purified talin was also phosphorylated by PK-P in a phospholipid-stimulable manner, but at 1/20 the rate of the 47-kD fragment.

Electropherogram pattern similarity of seed proteins from 21 different soybean (Glycine max) varieties

1977 ◽  
Vol 55 (16) ◽  
pp. 2245-2250 ◽  
Author(s):  
Clifton F. Savoy
Keyword(s):  
Glycine Max ◽  
Seed Protein ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Plant Proteins ◽  
Relative Mobility ◽  
Molecular Weights ◽  
Pattern Similarity ◽  
Protein Components ◽  
Phosphate Detergent

Soybean (Glycine max) seed protein has been characterized using a phosphate-detergent (sodium dodecyl sulfate) polyacrylamide gel electrophoretic system, which has been extensively tested on plant proteins. The same general densitometer electropherogram pattern as regards numbers and kinds of protein components resolved was observed for all soybean varieties tested, and one pattern is presented along with appropriate descriptive characterizations (numbers, molecular weights, relative mobility, and light absorption at 597 nm) to aid in distinguishing the components. Quantitative differences, however, of individual components may occur.

scholarly journals THE ISOLATION OF MOUSE HEPATOCYTE GAP JUNCTIONS

1972 ◽  
Vol 54 (3) ◽  
pp. 646-656 ◽  
Author(s):  
Daniel A. Goodenough ◽  
Walther Stoeckenius
Keyword(s):  
Gap Junctions ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Hexagonal Lattice ◽  
Major Protein ◽  
X Ray Diffraction ◽  
Thin Sectioning ◽  
Staining Techniques ◽  
Minor Phospholipid ◽  
Sucrose Gradient Ultracentrifugation

A method is reported for isolating a preparation of hepatic gap junctions from the mouse. The method involves a collagenase digestion, treatment with the detergent Sarkosyl NL-97, and ultrasonication, followed by sucrose gradient ultracentrifugation. A run with 36 animals yields 0.1–0.5 mg protein. Electron microscopy with thin-sectioning and negative staining techniques reveals that the final pellet is a very pure preparation of gap junctions, accompanied by a small amount of amorphous contamination. Polyacrylamide-gel electrophoresis of sodium dodecyl sulfate (SDS)-solubilized material shows one major protein in the junction, with an apparent mol wt of 20,000, and two minor components. Thin-layer chromatography demonstrates one major and one minor phospholipid, and some neutral lipid. Low-angle X-ray diffraction of wet and dried specimens show reflections which index on an 86 A center-to-center hexagonal lattice, corresponding closely to electron microscope data. Dried specimens also show a lamellar diffraction, corresponding to the total profile thickness of the junction (150 A).

Partial purification and characterization of isopenicillin N epimerase activity from Streptomyces clavuligerus

1983 ◽  
Vol 29 (11) ◽  
pp. 1526-1531 ◽  
Author(s):  
Susan E. Jensen ◽  
Donald W. S. Westlake ◽  
Saul Wolfe
Keyword(s):  
Pyridoxal Phosphate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Streptomyces Clavuligerus ◽  
Enzymic Activity ◽  
Partial Purification ◽  
Major Protein ◽  
Major Protein Band ◽  
Isopenicillin N

Epimerase activity, which converts isopenicillin N to penicillin N, has been partially purified from cell-free extracts of Streptomyces clavuligerus. No stimulating cofactors of this activity were found, and neither EDTA nor anaerobic incubation caused significant inhibition of activity. Although pyridoxal phosphate did not stimulate epimerase activity, the presence of this cofactor was necessary for the stabilization of enzymic activity during the purification process. Epimerase activity was purified 35.5-fold by a combination of salt precipitation, gel filtration, and ion exchange chromatography. Gel filtration indicated that the epimerase has a molecular weight of 60 000 and sodium dodecyl sulphate – polyacrylamide gel electrophoresis of the 35.5-fold purified epimerase showed a major protein band running near that location. Pyridoxal phosphate antagonists did not uniformly inhibit epimerase activity, but the inhibitory effect of hydroxylamine could be partially reversed by pyridoxal phosphate.

scholarly journals Identification of the Nucleocapsid, Tegument, and Envelope Proteins of the Shrimp White Spot Syndrome Virus Virion

2006 ◽  
Vol 80 (6) ◽  
pp. 3021-3029 ◽  
Author(s):  
Jyh-Ming Tsai ◽  
Han-Ching Wang ◽  
Jiann-Horng Leu ◽  
Andrew H.-J. Wang ◽  
Ying Zhuang ◽  
...  
Keyword(s):  
White Spot Syndrome Virus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Envelope Proteins ◽  
White Spot ◽  
Structural Proteins ◽  
Nucleocapsid Proteins ◽  
Tegument Proteins ◽  
White Spot Syndrome ◽  
Protein Components

ABSTRACT The protein components of the white spot syndrome virus (WSSV) virion have been well established by proteomic methods, and at least 39 structural proteins are currently known. However, several details of the virus structure and assembly remain controversial, including the role of one of the major structural proteins, VP26. In this study, Triton X-100 was used in combination with various concentrations of NaCl to separate intact WSSV virions into distinct fractions such that each fraction contained envelope and tegument proteins, tegument and nucleocapsid proteins, or nucleocapsid proteins only. From the protein profiles and Western blotting results, VP26, VP36A, VP39A, and VP95 were all identified as tegument proteins distinct from the envelope proteins (VP19, VP28, VP31, VP36B, VP38A, VP51B, VP53A) and nucleocapsid proteins (VP664, VP51C, VP60B, VP15). We also found that VP15 dissociated from the nucleocapsid at high salt concentrations, even though DNA was still present. These results were confirmed by CsCl isopycnic centrifugation followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and liquid chromatography-nanoelectrospray ionization-tandem mass spectrometry, by a trypsin sensitivity assay, and by an immunogold assay. Finally, we propose an assembly process for the WSSV virion.

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