PEROXIDASE ZYMOGRAMS OF 16 APPLE ROOTSTOCKS

1986 ◽  
Vol 66 (3) ◽  
pp. 647-652 ◽  
Author(s):  
DAVID L. WELLER ◽  
JOSEPH F. COSTANTE
Keyword(s):  
Malus Domestica ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Apple Rootstocks ◽  
Malus Domestica Borkh ◽  
Root Extracts

Shoot bark and root extracts of 16 different apple (Malus domestica Borkh.) root-stocks were analyzed for multiple electrophoretic forms of peroxidase (EC 1.11.1.7) using polyacrylamide gel electrophoresis (PAGE). Thirteen bands were seen in the peroxidase zymograms of shoot bark extracts and eight in the peroxidase zymograms of root extracts. The root peroxidase bands corresponded to ones in the shoot bark peroxidase zymograms. Two of the bands were common to all 16 rootstock patterns. The other 11 bands formed six patterns which were characterized by the presence of specific peroxidase bands. The 16 rootstocks were grouped according to banding characteristics.Key words: Apple, Malus domestica Borkh., apple rootstocks, PAGE-peroxidase zymograms

scholarly journals Studies on Platelet Glycoproteins by Surface Labeling and SDS Polyacrylamide Gel Electrophoresis

1977 ◽  
Author(s):  
I. Hagen ◽  
N.O. Solum ◽  
M. Peterka
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Conformational State ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Metabolic Inhibitors ◽  
Conventional System ◽  
Platelet Surface ◽  
Release Reaction

Platelet surface (glyco)proteins, and alterations in these in connection with the thrombin-induced release reaction has been studied. Platelets were labeled by lactoperoxidase-catalyzed iodination, and examined by SDS gel electrophoresis in two different gel systems, one conventional(J. Biol. Chem.1969 244 4406), and the other containing urea and EDTA in the gels. In the conventional system the bulk of radioactivity coincided with a PAS band (GP III) of MW about 100, 000. In the other system, the main radioactive peak appeared in the GP II area (MW 120,000), and a shift in the PAS stain intensity from GP III to GP II was seen. Thrombasthenic platelets showed only traces of the GP II band in both systems. The bulk of radioactivity was associated with the surface glycopolypeptide GPS, which is present, but not labeled in normal platelets. In thrombin-released platelets, GPS in its unreduced state has an altered electrophoretic mobility compared to control platelets and platelets which have been incubated with metabolic inhibitors to prevent secretion. The findings indicate that the GP III band consists of two different polypeptides, one of which appears in the GP II area in gels containing urea and EDTA. Further, that thrombasthenic platelet membrane exists in a conformational state different from that of normal platelets. And finally, GPS is in some way involved in, or influenced by, the thrombin-induced release reaction.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

Inheritance and linkage relationships of seed peroxidase loci in hexaploid oat (Avena sativa L.)

Genome ◽  
1995 ◽  
Vol 38 (3) ◽  
pp. 467-471
Author(s):  
N. R. Sharopova ◽  
A. A. Sozinov ◽  
V. A. Portyanko
Keyword(s):  
Avena Sativa ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Linkage Groups ◽  
Peroxidase Isozyme ◽  
Linkage Relationships

Polyacrylamide gel electrophoresis has been used to investigate the inheritance and linkage relationships between anodal (PXA) and cathodal (PXC) seed peroxidases in hexaploid oat (Avena sativa L.). A total of 12 seed peroxidase loci (5 loci of PXA and 7 loci of PXC) were identified in three crosses. Only two Pxc loci (Pxc5 and Pxc7) were not linked to any peroxidase loci; the others were scored in three linkage groups. The order of the three loci assigned to one of the linkage groups was Pxc1–Pxa5–Pxc2. The order of loci in the other two linkages were Pxc4–Pxa1–Pxa3 and Pxc3–Pxa4–Pxa2. Also, the Pxc6 locus was shown to be linked to the Pxc3 locus. Considering that A. sativa is an allohexaploid, it can be proposed that the three peroxidase linkages represent homoeologous chromosomes.Key words: seed peroxidase, isozyme inheritance, linkage, Avena sativa.

An Evaluation of a Simple Polyacrylamide Gel Electrophoresis System for Lipoproteins and its Use for the Characterisation of Hyperlipoproteinaemia

1979 ◽  
Vol 16 (1-6) ◽  
pp. 44-46 ◽  
Author(s):  
Ying Foo ◽  
T. R. Tickner ◽  
D. G. Cramp
Keyword(s):  
Total Cholesterol ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Screening Procedure ◽  
Agarose Gel ◽  
Chemical Profile ◽  
Visual Appearance ◽  
Electrophoresis System

The use of polyacrylamide gel electrophoresis as a screening procedure for the characterisation of hyperlipoproteinaemia is described. Sixty-one samples were investigated and classified by four different methods: (1) chemical profile derived from visual appearance and estimation of total cholesterol and triglyceride; (2) ‘SML’ profile by nephelometry; (3) electrophoresis on agarose gel; and (4) electrophoresis on polyacrylamide gel. Polyacrylamide gel electrophoresis showed the closest correlation with the chemical profile when compared with the other two methods. Polyacrylamide gel electrophoresis was found to be a rapid, reliable, and satisfactory procedure for plasma lipoprotein phenotyping.

Detection of Low Molecular Size Lipopolysaccharide Contaminated in Dialysates used for Hemodialysis Therapy with Polyacrylamide Gel Electrophoresis in the Presence of Sodium Deoxycholate

1993 ◽  
Vol 16 (5) ◽  
pp. 245-248 ◽  
Author(s):  
T. Komuro ◽  
R. Nakazawa
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Aqueous Media ◽  
Molecular Size ◽  
Sodium Deoxycholate ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Bacterial Endotoxin ◽  
Molecular Sizes ◽  
Dialysis Membranes

Dialysis membranes are generally considered to be impermeable for bacterial endotoxin (lipopolysaccharide, LPS) contaminated in dialysates used for hemodialysis therapy, since LPS molecular size in aqueous media has been reported to be more than 106. However, there are few reports concerning its size in dialysates. We have already presented a newly developed polyacrylamide gel electrophoresis with sodium deoxycholate (DOC-PAGE) which proves the LPS size. Using this method, therefore, we attempted to clarify the size of LPS in dialysates. We demonstrated that LPS in dialysates had roughly two different molecular sizes with DOC-PAGE and that compared to migration profiles of Salmonella LPS as controls on DOC-PAGE, one molecular size of LPS was approximately 4,000 and the other in tens of thousands. This investigation indicates the possibility of LPS transfer across dialysis membranes.

scholarly journals Characterisation of oat genetic resources using electrophoresis of avenins

2011 ◽  
Vol 47 (No. 4) ◽  
pp. 166-171 ◽  
Author(s):  
I. Polišenská ◽  
L. Nedomová ◽  
T. Vyhnánek
Keyword(s):  
Czech Republic ◽  
Genetic Resources ◽  
Avena Sativa ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
The Czech Republic ◽  
Oat Breeding

The prolamin (avenin) patterns of  oat (Avena sativa L.) cultivars released in  the Czech Republic and in the former Czechoslovak Republic were analysed  by acid polyacrylamide gel electrophoresis (A-PAGE).  Forty-nine oat (Avena sativa L.) accessions of domestic origin, maintained in the Czech collection of oat genetic resources, were analysed. The evaluated set contained 18 modern  and 31 old cultivars. Thirty accessions showed a homogeneous prolamin pattern. The other accessions were heterogeneous with two or three different patterns, present at different percentages. Heterogeneity was present in 48% of the old cultivars, but  only in 22% of the modern cultivars. Identity indexes within the heterogeneous accessions were calculated. The index values ranged from 0.09 to 0.75. Only in two heterogeneous cultivars (Dětenický Bílý, Valečovský Bílý) the identity index between their components was higher than 0.6, indicating, that their components were most likely sister lines. All analysed cultivars could be unambiguously distinguished by their prolamin pattern. The obtained prolamin patterns will be used to complete descriptor data of the genetic resources  and might be useful also in oat breeding and research. 

Interactions between Factors XII and XI and Activating Agents in Purified Systems

1975 ◽  
Author(s):  
B. Binder ◽  
G. Krug ◽  
Th. Vukovich
Keyword(s):  
Complex Formation ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Coagulation Factors ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Ionic Exchange ◽  
Solid Complex ◽  
No Activation

To obtain a better understanding of the activating mechanism of F XI we studied the interaction of highly purified F XII and F XI with activating agents (kaolin, cephalin) F XII as well as F XI were purified from ACD-plasma (ionic exchange procedures, gel fractionation). Both coagulation factors were obtained with a specific activity per mg protein of approximately 4000 times the value of the original plasma, showing a single band in polyacrylamide gel electrophoresis. The preparations contained less than 1 per cent of their activated forms.F XII and F XI as well as the mixture of both were exposed to kaolin, cephalin, or a kaolin-cephalin mixture, respectively. F XII was adsorbed to about 90 per cent by kaolin alone and the adsorbed fraction was activated completely within minutes; F XI on the other hand was neither adsorbed nor activated by kaolin. The kaolin-activated F XII effected practically no activation of F XI. By cephalin F XII was activated only within hours, but the so activated F XII produced activation of F XI corresponding to F XIIa available in a ratio F XIIa/F XI a of 10/1. A mixture of kaolin and cephalin activated F XII within minutes; ca 20 to 30 per cent of the resulting F XIIa activity became not adsorbed to kaolin and this F XII a activates F XI in the same ratio as in the case of cephalin-activated F XII. Gel fractionation of F XII and F XI together with cephalin revealed that only F XIIa is bound to the phospholipid; no solid complex formation was found between F XI and cephalin or between F XI and F XII.(Supp. by a Grant from the Eisner-Foundation.)

Isoenzyme and protein patterns of pentose-fermenting yeasts

1987 ◽  
Vol 33 (11) ◽  
pp. 1017-1023 ◽  
Author(s):  
Robert S. Jeng ◽  
Shiyuan Yu ◽  
Morris Wayman
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Pichia Stipitis ◽  
Culture Collection ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Two Dimensional ◽  
Protein Patterns

Soluble proteins were extracted from the vegetative cells of four pentose-fermenting yeasts, Candida shehatae, Pichia stipitis, R-1, and R-2, the R strains being of uncertain taxonomy, while the other two are culture collection yeasts. Isoenzyme patterns, protein patterns, and two-dimensional polypeptide mapping of these four strains were compared by polyacrylamide gel electrophoresis. The two R strains showed great similarity in two-dimensional polypeptide mapping, the pattern of sodium dodecyl sulfate – polyacrylamide gel electrophoresis, isoelectrofocusing, and isoenzymes, and may be one species. Each of the other two yeasts had its own characteristic electrophoretic pattern. The R strains showed the presence of three alcohol dehydrogenase isoenzymes compared with one for the culture collection yeasts, as well as much higher activity of malate dehydrogenase, isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase, which further the formation of pyruvate and ethanol.

Differentiation of Rennet from Other Milk-Clotting Enzymes by Polyacrylamide Gel Electrophoresis

1977 ◽  
Vol 60 (6) ◽  
pp. 1372-1374 ◽  
Author(s):  
Manfred J Prager
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Characteristic Pattern ◽  
Aniline Blue ◽  
Major Protein ◽  
Milk Clotting ◽  
Microbial Origin

Abstract Polyacrylamide gel electrophoresis was used to differentiate animal rennet and other milk-clotting enzymes. After electrophoresis, the separated components were visualized by staining with aniline blue-black. Two prominent proteins were found in calf and bovine rennet, while only 1 major protein was observed in pepsin and enzymes of microbial origin. These patterns provided a basis for distinguishing animal rennet and the other enzymes as well as a means of identifying each type of enzyme by the characteristic pattern shown.

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).

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