Molecular weight and net charge of peroxidase isozymes in F1 hybrids between L and S flax genotrophs

1982 ◽  
Vol 20 (9-10) ◽  
pp. 919-927 ◽  
Author(s):  
Hugh Tyson ◽  
Mary Ann Fieldes
Keyword(s):  
Molecular Weight ◽  
F1 Hybrids ◽  
Net Charge ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs

DIFFERENCES IN MOLECULAR WEIGHT BETWEEN CORRESPONDING ANIONIC PEROXIDASE ISOZYMES FROM TWO FLAX GENOTROPHS

1980 ◽  
Vol 22 (4) ◽  
pp. 529-534 ◽  
Author(s):  
H. Tyson ◽  
M. A. Fieldes
Keyword(s):  
Molecular Weight ◽  
Linear Regression ◽  
Linum Usitatissimum ◽  
Gel Electrophoresis ◽  
Relative Mobility ◽  
Anionic Peroxidase ◽  
Linum Usitatissimum L ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Adult Plants

Anionic peroxidase isozymes from main stem tissues of adult plants of two flax (Linum usitatissimum L.) genotrophs were separated using acrylamide gel electrophoresis. A range of seven acrylamide concentrations was used for the gels, enabling the effect of gel concentration on relative mobility (Rm) to be examined. The regression of log (Rm) on gel concentration was linear for two of the four main isozymes found. Differences in linear regression slope between the L and S flax genotroph isozymes suggested genotroph differences in molecular weight.

scholarly journals Preliminary characterization of peroxidase isozymes isolated from two flax genotrophs

1977 ◽  
Vol 55 (11) ◽  
pp. 1465-1473 ◽  
Author(s):  
M. A. Fieldes ◽  
C. L. Deal ◽  
H. Tyson
Keyword(s):  
Molecular Weight ◽  
Oxidase Activity ◽  
Indoleacetic Acid ◽  
Relative Mobility ◽  
Fresh Weight ◽  
Iaa Oxidase ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Very High

Four peroxidase (EC 1.11.1.7) isozymes were isolated from each of two flax genotrophs. All four isozymes were glycoproteins and all exhibited indoleacetic acid (IAA) oxidase activity. The percentage purity of two of the isozymes was very high; these isozymes differed in percentage carbohydrate and in peroxidase and IAA oxidase specific activities. Three of the isozymes displayed molecular weight values of about 43 000; for the fourth, molecular weight was considerably higher. Corresponding isozymes from the genotrophs and from two other flax genotypes displayed molecular weight differences which corresponded to electrophoretic relative mobility differences. Enzyme yield per unit fresh weight was higher for one genotroph than the other, and the balance between peroxidase activity and IAA oxidase activity between the genotrophs was different.

Evidence for heterogeneity in the carbohydrate moieties of peroxidase isozymes from two environmentally induced flax genotrophs

1986 ◽  
Vol 64 (11) ◽  
pp. 2682-2687 ◽  
Author(s):  
Pierre-Richard Gaudreault ◽  
Hugh Tyson
Keyword(s):  
Molecular Weight ◽  
Affinity Chromatography ◽  
Concanavalin A ◽  
Posttranslational Modification ◽  
Stem Tissue ◽  
Carbohydrate Composition ◽  
Molecular Weights ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Carbohydrate Chains

The corresponding isoperoxidases from the flax genotrophs L and S have different molecular weights. Utilizing affinity chromatography on Sepharose-bound concanavalin A, we have shown that this lectin has a stronger affinity for the isoperoxidases purified from S stem tissue than those from L. The presence of differences in the carbohydrate composition of L and S peroxidases was confirmed when it was observed that only S peroxidases were susceptible to digestion by endo-β-N-acetylglucosaminidase H. Glycoprotein-enriched fractions were then purified from L and S stem tissue. The results showed that most glycoproteins of S origin have higher molecular weights than their L counterparts. Certain glycoproteins were digested by endo-β-N-acetylglucosaminidase H only if they were of S origin, while others were digested regardless of their origin. In both cases, the original differences in molecular weight between L and S glycoproteins were eliminated. These results support our view that posttranslational modification at the level of the carbohydrate chains of the L and S peroxidases is the reason for their heterogeneity on polyacrylamide gels.

COMPARATIVE THERMAL STABILITY OF PEROXIDASE ISOZYMES FROM TWO FLAX GENOTROPHS

1982 ◽  
Vol 24 (4) ◽  
pp. 427-435 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson
Keyword(s):  
Thermal Stability ◽  
Molecular Weight ◽  
Prolonged Treatment ◽  
Linum Usitatissimum L ◽  
Peroxidase Isozymes ◽  
Heat Treated ◽  
Peak Areas ◽  
Flax Genotrophs ◽  
Thermal Stability Of

The thermal stability of peroxidase isozymes was examined in vitro in Linum usitatissimum L. Extracts of main stem tissues of the L and S genotrophs produced by Durrant were heat treated over a range of temperatures and times. Isozymes in treated extracts were separated electrophoretically, and peak areas for the four main anionic isozymes, together with their relative mobilities (Rms), were recorded. Peak areas supplied estimates of relative activities. Short duration treatments at 60° and 70 °C demonstrated differences in thermal stability between isozymes and produced changes in Rm. With prolonged treatment at 40 °C, the thermal stability of one isozyme differed from those of the other three. This isozyme was known to have a higher molecular weight than the others. In addition, prolonged treatment at 40 °C demonstrated increased thermal stability of the three lower molecular weight isozymes of genotroph S compared to those of L.

Molecular weight differences in acid phosphatases of stem homogenates from L and S flax genotrophs

1983 ◽  
Vol 21 (3-4) ◽  
pp. 391-404 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatases ◽  
Flax Genotrophs

Structural Elements Which Govern the Resistance of Intestinal Tissues to Compound Transport

1993 ◽  
Vol 331 ◽  
Author(s):  
Werner Rubas ◽  
Mary Cromwell ◽  
Tom Gadek ◽  
Daljit Narindray ◽  
Randy Mrsny
Keyword(s):  
Molecular Weight ◽  
Reversed Phase ◽  
Paracellular Pathway ◽  
Structural Elements ◽  
Reversed Phase Hplc ◽  
Net Charge ◽  
Rgd Peptides ◽  
Paracellular Shunt ◽  
Charge Interactions

The series of cyclized RGD peptides in this study demonstrated a very low partition into octanol as judged by HPLC. Thus, these molecules are likely to move predominantly through the paracellular pathway. Permeability across Caco-2 monolayers was determined using reversed phase HPLC and found to be restricted by molecular weight and possibly charge-charge interactions between the solute and charged moieties within the paracellular shunt. When normalized for molecular weight, molecules with a net charge between -1 and -2 demonstrated the highest permeabilities, which suggests an optimal net charge with respect to permeability.

scholarly journals Presence of histones in Aspergillus nidulans.

1976 ◽  
Vol 68 (3) ◽  
pp. 430-439 ◽  
Author(s):  
R A Felden ◽  
M M Sanders ◽  
N R Morris
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Amino Acid Analysis ◽  
Gel Chromatography ◽  
Mobility Patterns ◽  
Net Charge ◽  
Basic Proteins ◽  
Calf Thymus

Five major histone proteins have been extracted from chromatin isolated from purified nuclei of the fungus, Aspergillus nidulans. These proteins had chromatographic properties which were similar to reference calf thymus histones and were purified to electrophoretic homegeneity by gel chromatography of Bio-Gel P10, Bio-Gel P60, and Sephadex G-100. Electrophoresis of these proteins in three different systems (urea-starch, urea-acetic acid polyacrylamide, and discontinuous SDS polyacrylamide) showed that the A. nidulans histones H3 and H4 were nearly identical to calf thymus H3 and H4 with respect to net charge and molecular weight criteria, whereas the fungal histones H1, H2a and H2b were similar but not identical to the corresponding calf thymus histones. Amino acid analysis of A. nidulans histones H2a, H2b, and H4 showed them to be closely related to the homologous calf thymus histones. The mobility patterns of A. nidulans ribosomal basic proteins in three different electrophoretic systems were distinctly different from those of the fungal histones.

THE ELASTIC FIBER A REVIEW

1973 ◽  
Vol 21 (3) ◽  
pp. 199-208 ◽  
Author(s):  
RUSSELL ROSS
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Elastic Properties ◽  
Lysyl Oxidase ◽  
Elastic Fiber ◽  
Net Charge ◽  
Amorphous Component ◽  
Cross Links

A number of important questions remain to be answered concerning our understanding of elastic tissues. The size and molecular weight of the elastin precursor remains to be clearly established. The number of proteins involved in the microfibrillar component of the elastic fiber are as yet undetermined, although it would appear that they are glycoproteins that may represent a species of reasonably high molecular weight. Clearly the elastic fiber contains two morphologic components. During morphogenesis, the elastic fiber begins to appear in the form of aggregates of microfibrils that take the shape and direction of the presumptive elastic fiber. With increasing maturity elastin begins to form within the interstices of each bundle of microfibrils. By the time the elastic fiber is fully formed it consists largely of the amorphous component, elastin, surrounded by an envelope of microfibrils with microfibrils embedded within its interstices. It has been suggested that the microfibrils form and take their shape extracellularly under the influence of the cells that have secreted their precursors. After the aggregates of microfibrils have taken their shape Ross and Bornstein (22) have suggested that the elastin may interact ionically with the surface of the microfibrils, since each of these two components has an opposite net charge, and may be held in position while desmosine cross-links are established through the action of the enzyme, lysyl oxidase. Thus the microfibrils would serve as a scaffolding to determine morphogenetically the shape and direction to be later taken by the mature elastic fiber. The reason for the elastic properties of the elastin is still yet poorly understood, and the means by which the cells synthesize and secrete both of these components remain to be investigated.

scholarly journals Actin filaments in the acrosomal reaction of Limulus sperm. Motion generated by alterations in the packing of the filaments.

1975 ◽  
Vol 64 (2) ◽  
pp. 289-310 ◽  
Author(s):  
L G Tilney
Keyword(s):  
Molecular Weight ◽  
Actin Filaments ◽  
Heavy Meromyosin ◽  
Stable States ◽  
Equimolar Ratio ◽  
Net Charge ◽  
Molecular Weights ◽  
Acrosomal Reaction ◽  
Sperm Motion ◽  
Filament Bundle

When Limulus sperm are induced to undergo the acrosomal reaction, a process, 50 mum in length, is generated in a few seconds. This process rotates as it elongates; thus the acrosomal process literally screws through the jelly of the egg. Within the process is a bundle of filaments which before induction are coiled up inside the sperm. The filament bundle exists in three stable states in the sperm. One of the states can be isolated in pure form. It is composed of only three proteins whose molecular weights (mol wt) are 43,000, 55,000, and 95,000. The 43,000 mol wt protein is actin, based on its molecular weight, net charge, morphology, G-F transformation, and heavy meromyosin (HMM) binding. The 55,000 mol wt protein is in equimolar ratio to actin and is not tubulin, binds tenaciously to actin, and inhibits HMM binding. Evidence is presented that both the 55,000 mol wt protein and the 95,000 mol wt protein (possibly alpha-actinin) are also present in Limulus muscle. Presumably these proteins function in the sperm in holding the actin filaments together. Before the acrosomal reaction, the actin filaments are twisted over one another in a supercoil; when the reaction is completed, the filaments lie parallel to each other and form an actin paracrystal. This change in their packing appears to give rise to the motion of the acrosomal process and is under the control of the 55,000 mol wt protein and the 95,000 mol wt protein.

Peroxidase activity and relative mobility at anthesis in flax genotrophs and their F2 progeny: developmental and genetic effects

Genome ◽  
1991 ◽  
Vol 34 (4) ◽  
pp. 495-504 ◽  
Author(s):  
M. A. Fieldes ◽  
J. Ross
Keyword(s):  
Genetic Control ◽  
Peroxidase Activity ◽  
Stem Elongation ◽  
Genetic Regulation ◽  
Relative Mobility ◽  
Activity Data ◽  
Peroxidase Isozymes ◽  
Developmental Age ◽  
Total Peroxidase Activity ◽  
Flax Genotrophs

The genetic regulation of the environmentally induced heritable difference in peroxidase activity between Durrant's large (L) and small (S) flax genotrophs was examined in leaves from plants ranging in developmental age from 6 days before anthesis to 3 days after. Mean peroxidase activity was higher for S than L and intermediate for the reciprocal F2's from L × S and S × L crosses (F2L × S and F2S × L). However, activity increased with development and, since there were small but significant differences in the average developmental ages of L, S, F2L × S, and F2S × L plants, the effects of development on activity had to be taken into account in examining the F2 activity data for segregation. A regression method was used to remove developmental effects and, underlying these effects, total peroxidase activity appeared to be regulated by a single locus with two alleles and L dominance. Two other dimorphic loci, both described previously, were also examined. One regulates the presence-absence of septa hairs in the seed capsules and the other the relative mobility of anionic peroxidase isozymes. There was no phenotypic linkage between the three segregating parameters. The genetic control of activity appeared to regulate cationic rather than anionic activity. In addition, a relationship between activity and plant height indicated either that peroxidase activity is one of the factors regulating main stem elongation or that the locus regulating peroxidase activity is linked to one of the loci involved in the regulation of plant height.Key words: flax genotrophs, peroxidase, genetic control, development.

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