Changes in isoenzyme patterns during imbibition and germination of lodgepole pine (Pinuscontorta var. latifolia)

1984 ◽  
Vol 14 (5) ◽  
pp. 743-746 ◽  
Author(s):  
J. A. Pitel ◽  
W. M. Cheliak ◽  
B. S. P. Wang
Keyword(s):  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Lodgepole Pine ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Glutamate Oxaloacetate Transaminase ◽  
Major Band ◽  
Tissue Specific ◽  
Isoenzyme Patterns

Isoenzymes of esterase (EST), glutamate-oxaloacetate transaminase (GOT), leucine aminopeptidase (LAP), and peroxidase (PER) were examined following various periods of imbibition and germination of lodgepole pine (Pinuscontorta var. latifolia Engelm.) seeds. The acidic and basic isoenzymes of embryos, and roots and shoots of germinating seedlings were analyzed by polyacrylamide gel electrophoresis. One major band of EST disappeared with imbibition, while some minor bands appeared and disappeared with imbibition and germination. Comparison of the roots and shoots after 7 and 14 days of germination showed several tissue-specific differences. The number of bands of GOT increased with imbibition and germination. The levels of activity of three isoenzymes differed between the root and shoot tissues. One band of LAP disappeared with imbibition. The levels of activity of two bands varied between the root and shoot tissues. The number of bands of PER increased dramatically following imbibition and germination. Also, many tissue-specific differences were observed between root and shoot tissues.

scholarly journals Synthesis and secretion of alpha2-macroglobulin by cultured human fibroblasts.

1976 ◽  
Vol 143 (2) ◽  
pp. 462-467 ◽  
Author(s):  
D F Mosher ◽  
D A Wing
Keyword(s):  
Gel Electrophoresis ◽  
Human Fibroblasts ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Serum Free Medium ◽  
Free Medium ◽  
Major Band ◽  
Serum Free ◽  
Cultured Human Fibroblasts

The following observations indicate that cultured human WI-38 fibroblasts synthesize and secrete alpha2-macroglobulin into serum-free medium: (a) after incubation of cultures with [35S]L-methionine, a labeled protein appeared in the medium which was precipitated by antiserum directed against alpha2-macroglobulin; (b) after incubation of cultures with [35S]L-methionine, a major band of radioactivity detected by polyacrylamide gel electrophoresis of the proteins in medium co-migrated with alpha2-macroglobulin; and (c) the amount of alpha2-macroblobulin in the medium, estimated both functionally and immunologically, increased with time in normal but not not puromycin-treated cultures.

Isoenzymes of chloroperoxidase from Caldariomyces fumago

1982 ◽  
Vol 28 (12) ◽  
pp. 1382-1388 ◽  
Author(s):  
Michael A. Pickard ◽  
Atsumi Hashimoto
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Media Analysis ◽  
Polyacrylamide Gel ◽  
Prolonged Storage ◽  
Malt Extract ◽  
Major Band ◽  
Dodecyl Sulfate

Chloroperoxidase (EC 1.11.1.10) was purified from Caldaromyces fumago strains ATCC 16373 and CM1 89362 grown in defined and complex media. Analysis of the enzyme by polyacrylamide gel electrophoresis at pH 3, sodium dodecyl sulfate – polyacrylamide gel electrophoresis, and isoelectric focussing in polyacrylamide gels revealed two forms of the enzyme, the major form representing greater than 80% of the total protein. When the fungi were grown in synthetic media, more of the enzyme was found in the major band than when the fungi were grown in the presence of malt extract. Enzyme activity was demonstrated both by staining gels in situ with 3,3′,5,5′-tetramethylbenzidine and by spectrophometric assay of material eluted from gel slices. There were no obvious differences between the enzyme from C. fumago ATCC 16373 and from C. fumago CMI 89362. Commercial samples, included for comparative purposes, contained three or four enzymically active species which separated on polyacrylamide gel electrophoresis at pH 3 and electrofocussing but migrated as a close double band on sodium dodecyl sulfate – polyacrylamide gel electrophoresis. It is believed that prolonged storage in the unfrozen state is responsible for the conversion to multiple forms.

scholarly journals Proteins of the kidney microvillus membrane. Identification of subunits after sodium dodecylsullphate/polyacrylamide-gel electrophoresis

1976 ◽  
Vol 159 (2) ◽  
pp. 395-407 ◽  
Author(s):  
A G Booth ◽  
A J Kenny
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Neutral Endopeptidase ◽  
Polyacrylamide Gel ◽  
British Library ◽  
Major Band ◽  
Microvillus Membrane

The proteins of microvilli prepared from pig kidney were analysed by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. The typical pattern stained for protein revealed five major bands, four of which also stained for carbohydrate, and about 15 minor bands. For descriptive purposes the bands were designated numerically by their apparent molecular weights (X10(-3). Well-characterized proteins were identified with four of the five major bands. Dipeptidyl peptidase IV, a serine proteinase that may be specifically labelled with di-isopropyl [32P]phosphorofluoridate, was assigned to band 130. Aminopeptidase M was assigned to band 160, though when released from the membrane by a proteinase, this protein comprises three polypeptides each of lower apparent molecular weight than the native enzyme. Neutral endopeptidase can be assigned to band 95 and actin to band 42. The fifth major band (180) is an extrinsic glycoprotein that has not been identified with any microvillus enzyme activity. These four proteins contribute 21% of the microvillus-membrane protein. Kidney microvillus actin was characterized by a variety of properties and was similar to muscle actin. A computer analysis of the gel pattern indicates that it comprises 9.0% of the microvillus protein. Myosin is not present in the microvillus, but another protein associated with band 95, with properties that distinguish it from neutral endopeptidase, was tentatively identified as α-actinin. Alkaline phosphatase was identified as a monomeric polypeptide with an apparent molecular weight of 80000; it is a minor protein of the microvillus and is not discernible as a discrete band in the gel pattern. These and other results permit a model of the organization of the microvillus protein to be suggested. The computer program used has been deposited as Supplementary Publication SUP 50070 (12 pages) at the British Library Lending Division, Boston Spa. Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1976) 153,5.

Phylogenetic study and analysis of similarities for different datepalm cultivars using electrophoretic isoenzymes

2016 ◽  
Author(s):  
Adil M. Alissa
Keyword(s):  
Saudi Arabia ◽  
Gel Electrophoresis ◽  
Date Palm ◽  
Leucine Aminopeptidase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Phylogenetic Study ◽  
Glutamate Oxaloacetate Transaminase ◽  
Genetic Origin ◽  
Similarity Method ◽  
Degree Of Similarity

Non-specific esterases, Glutamate Oxaloacetate Transaminase and Leucine-aminopeptidase isoenzymes were extracted from fifteen date palm cultivars in The Al-Ahsa oasis in Saudi Arabia, and subjected to analysis by polyacrylamide gel electrophoresis. The results revealed differences in the degree of similarity between the cultivars from 0.147 to 0.552, estimated according to Jaccard’s Similarity method on the basis of presence and absence of EST and GOT isoenzymes bands collectively. Grr, Hel and Shl cultivars were closely related within a mini-cluster with degrees of similarity from 0.400 to 0.519. Ruz and Ows cultivars were closely related to each other with 0.552 degree of similarity. Tyr, OmR and Asi cultivars were closely related within a sub-cluster with degrees of similarity from 0.357 to 0.440. Mj and Khs cultivars were closely related to each other with 0.500 degree of similarity. It could be concluded that the isoenzymes are informative and helpful in the discrimination between the cultivars, as well as the results support the conclusion that most of the The Al-Ahsa oasis date palm cultivars referred to one genetic origin.

Avian trypanosomes in Simulium and sparrowhawks(Accipiter nisus)

Parasitology ◽  
1990 ◽  
Vol 101 (2) ◽  
pp. 243-247 ◽  
Author(s):  
M. F. Dirie ◽  
R. W. Ashford ◽  
L. M. Mungomba ◽  
D. H. Molyneux ◽  
E. E. Green
Keyword(s):  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Defined Medium ◽  
Polyacrylamide Gel ◽  
Cellulose Acetate Electrophoresis ◽  
Accipiter Nisus ◽  
Large Numbers ◽  
Isoenzyme Patterns ◽  
Infected Prey

Isolates of avian trypanosomes from nestling sparrowhawks (Accipiter nisus) and from Simulium latipes were compared by isoenzyme electrophoresis with the previously described avian trypanosomes Trypanosoma corvi and T. everetti. Simulium isolates developed into trypomastigotes in semi-defined medium at 37 °C confirming that they belong to the genus Trypanosoma. Cellulose acetate electrophoresis (CAE) and polyacrylamide gel electrophoresis (PAGE) methods were employed. A total of 11 enzymes was examined, of which 8 gave satisfactory results for all lysates (MDH, ICD, PGM, 6PGD, SOD, PEP I, PEP II and PEP D). The zymograms of 3 isolates from Simulium and 4 from A. nisus were similar indicating that they were the same organism and the isoenzyme patterns coincided with those of T. corvi. It is concluded that A. nisus and S. latipes are infected with T. corvi. Flagellate infections were found in the midgut, hindgut and rectum of Simulium where large numbers of epimastigotes were found in the lumen and attached to the cuticular intima of the rectal ampullae by hemidesmosomes at the distal end of an expanded flagellum. Out of 285 nestling sparrowhawks 13 (5%) were infected with trypanosomes. In view of their age and inability to preen themselves it is suggested they became infected via infected prey.

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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