Cotyledonary Storage Proteins in Pisum sativum. I. Molecular Heterogeneity

1978 ◽  
Vol 5 (3) ◽  
pp. 263 ◽  
Author(s):  
JA Thomson ◽  
HE Schroeder ◽  
WF Dudman
Keyword(s):  
Cellulose Acetate ◽  
Electrophoretic Mobility ◽  
Storage Protein ◽  
Storage Proteins ◽  
Electrophoretic Analysis ◽  
Molecular Heterogeneity ◽  
Polypeptide Composition ◽  
Ph Values ◽  
Pea Seeds ◽  
Differential Solubility

The two storage-protein fractions of pea seeds, legumin and vicilin, have each been resolved electrophoretically on a cellulose acetate gel matrix into multiple molecular species distinguished by electrophoretic mobility and by quantitative or qualitative differences in subunit composition or both. Electrophoretograms of these apparent holoproteins from a range of lines and cultivars were found to be genotype-specific, generally showing three strong bands, together with up to three additional minor bands, assignable to a vicilin series of components. A further three or four bands could be assigned to a legumin series, although the slowest of these showed apparent admixture of certain polypeptides typical of the vicilin fractions. Each putative holoprotein band in both the legumin and vicilin series behaved additively in the electrophoretograms of F1 offspring from reciprocal crosses between lines showing distinct patterns. For comparison with the proteins distinguished electrophoretically on cellulose acetate gels, storage proteins from lyophilized protein bodies were fractionated on the basis of differential solubility at various ionic strengths and pH values. The single legumin and three vicilin fractions obtained by this method showed sedimentation velocities typical of the respective holoproteins. No overlap in the polypeptide composition of legumin with that of vicilin fractions was observed. The components represented in the four fractions accounted for all the major polypeptides in total storage-protein extracts and in the bands eluted from cellulose acetate gels. The distinctive polypeptide pattern and electrophoretic mobility of vicilin fraction 4 identified this protein as a contaminant of slow legumin bands in cellulose acetate gels, and as an additional vicilin species not recognized directly from the electrophoretic analysis.

Cotyledonary Storage Proteins in Pisum Sativum. II. Hereditary Variation in Components of the Legumin and Vicilin Fractions

1978 ◽  
Vol 5 (3) ◽  
pp. 281 ◽  
Author(s):  
JA Thomson ◽  
HE Schroeder
Keyword(s):  
Pisum Sativum ◽  
Phenotypic Variation ◽  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Gene Products ◽  
Hereditary Variation ◽  
Pea Seeds ◽  
Parental Lines ◽  
Variant System

Gel electrophoresis has been used to investigate genetically controlled variation in storage-protein constituents forming five series of bands (LA-LE) derived from legumin fractions, and three series of bands (VA-VC) from vicilin fractions, of pea seeds. In each variant system, the phenotypes of the storage-protein polypeptides from F1 seeds were additive with respect to the band patterns of the parental lines, and identical in reciprocal crosses. Neither dominance nor formation of new interaction products was observed. Variation in the three systems involving vicilin polypeptides and two of those involving legumin components was found to be based on allelic alternatives at single loci designated Vicilin A (Vca), Vicilin B (Vcb), Vicilin C (Vcc), Legumin A (Lga) and Legumin C (Lgc). For each of these variant systems, the gene products involved and the basis of the phenotypic variation have been discussed. Variants of the VC band complex, in which mobility of two bands both composed of 12 and 14 kdalton polypeptides is altered, appear likely to correspond to vicilin variants described previously. Type lines are specified for each of the variant phenotypes analysed, and for the genes designated.

Cotyledonary Storage Proteins in Pisum sativum. III. Patterns of Accumulation During Development

1978 ◽  
Vol 5 (4) ◽  
pp. 519 ◽  
Author(s):  
A Millerd ◽  
JA Thomson ◽  
HE Schroeder
Keyword(s):  
Antigenic Determinant ◽  
Storage Proteins ◽  
Subsequent Development ◽  
The Other ◽  
Polypeptide Composition ◽  
Crossed Immunoelectrophoresis ◽  
Antigen Present ◽  
Pea Seeds ◽  
Quantitative Changes ◽  
Change In Mean

An antiserum raised against proteins from isolated protein bodies of mature pea seeds recognized seven antigenically distinct protein families in cotyledon extracts analysed by crossed immunoelectrophoresis. This antiserum has been used to follow the sequence of appearance and pattern of accumulation of these proteins in peas grown under controlled environmental conditions. One antigen present in mature cotyledons was shown to be a haemagglutinin, one corresponded to legumin, and four distinct, non-crossreacting antigenic species were related to the vicilin series of proteins. Both the number of components detected and the order of their appearance during development were similar in three genotypes examined, but the quantitative representation of legumin relative to other components was genotype-specific. Quantitative differences were observed in the polypeptide composition of the vicilin components responsible for separate antigenic specificities, but qualitative differences were not excluded. During development, similar conspicuous quantitative changes in polypeptide composition, accompanied by a change in mean electrophoretic mobility, occurred amongst the molecules carrying the predominant antigenic determinant related to vicilin (peak 4); again, qualitative differences might also distinguish these components. The antigen responsible for peak 6 contained two major polypeptides distinct from the components of the legumin and vicilin fractions. Peak 6 represented the first fully immunocompetent species to appear during development, but later became quantitatively less significant as the other antigenic species accumuIated. Legumin and the antigen forming peak 6 were first detected immunologically in an apparently incomplete form. These putative precursors disappeared during subsequent development, so that only the corresponding stable precipitin peaks were seen in the immunoelectrophoretic profiles of extracts from mature cotyledons.

scholarly journals Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.)

1985 ◽  
Vol 225 (1) ◽  
pp. 239-247 ◽  
Author(s):  
J A Gatehouse ◽  
J Gilroy ◽  
M S Hoque ◽  
R R D Croy
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Amino Acid Sequence ◽  
Storage Protein ◽  
Seed Protein ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Pisum Sativum L ◽  
New Type ◽  
Pea Seeds

The seeds of pea (Pisum sativum L.) contain several proteins in the albumin solubility fraction that are significant components of total cotyledonary protein (5-10%) and are accumulated in developing seeds concurrently with storage-protein synthesis. One of these proteins, of low Mr and designated ‘Psa LA’, has been purified, characterized and sequenced. Psa LA has an Mr of 11000 and contains polypeptides of Mr 6000, suggesting that the protein molecules are dimeric. The amino acid sequence contains 54 residues, with a high content (10/54) of asparagine/aspartate. It has no inhibitory action towards trypsin or chymotrypsin, and is distinct from the inhibitors of those enzymes found in pea seeds, nor does it inhibit hog pancreatic alpha-amylase. The protein contains no methionine, but significant amounts of cysteine (four residues per polypeptide), suggesting a possible role as a sulphur storage protein. However, its sequence is not homologous with low-Mr (2S) storage proteins from castor bean (Ricinus communis) or rape (Brassica napus). Psa LA therefore represents a new type of low-Mr seed protein.

A STUDY OF A WATER-SOLUBLE COMPLEX OF PRODIGIOSIN PRODUCED BY A STRAIN OF SERRATIA MARCESCENS

1962 ◽  
Vol 40 (1) ◽  
pp. 1019-1024 ◽  
Author(s):  
Seiichi Yoshida
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Serratia Marcescens ◽  
Average Molecular Weight ◽  
Electrophoretic Analysis ◽  
Water Soluble ◽  
Soluble Complex ◽  
Ph Values ◽  
Scattering Measurements ◽  
Water Soluble Complex

A water-soluble pigment excreted from Serratia marcescens has been purified by precipitation with ammonium sulphate, dialysis, and ultracentrifugation at different pH values. The purified pigment showed a single band in the ultracentrifuge and by electrophoretic analysis at several pH values. An average molecular weight of 5 × 106 was calculated from light-scattering measurements. This pigment is composed of carbohydrate and protein combined with prodigiosin, and several properties of the complex are described.

Confirmation of a New Species of Small Dasyurid Marsupial by Electrophoretic Analysis of Enzymes and Proteins

1983 ◽  
Vol 31 (5) ◽  
pp. 743 ◽  
Author(s):  
DW Cooper ◽  
A Woolley
Keyword(s):  
New Species ◽  
Genetic Distance ◽  
Electrophoretic Mobility ◽  
Late Miocene ◽  
Electrophoretic Analysis ◽  
Early Pliocene ◽  
Antechinus Stuartii ◽  
A New Species ◽  
Nei's Genetic Distance

Eight species of dasyurid marsupials have been typed for the electrophoretic mobility of 18 of their enzymes and proteins. The species were the Ningbing antechinus (Pseudantechinus sp.), Pseudantechinus macdonnellensis (formerly Antechinus macdonnellensis), Parantechinus apicalis (formerly Antechinus apicalis), Parantechinus bilarni (formerly Antechinus bilarni), Antechinus stuartii, Dasykaluta rosamondae (formerly Antechinus rosamondae), Dasycercus cristicauda and Planigale maculata. The results show that the Ningbing antechinus is a probable new species. The data suggest that its nearest relative is Dasycercus cristicauda. Analysis of the results by calculation of a modified x2 and an approximation to Nei's genetic distance indicates that all species have been the product of one radiation, possibly in the late Miocene or early Pliocene. Two races of P. macdonnellensis probably exist, separable by their transferrin types.

A STUDY OF A WATER-SOLUBLE COMPLEX OF PRODIGIOSIN PRODUCED BY A STRAIN OF SERRATIA MARCESCENS

1962 ◽  
Vol 40 (8) ◽  
pp. 1019-1024 ◽  
Author(s):  
Seiichi Yoshida
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Serratia Marcescens ◽  
Average Molecular Weight ◽  
Electrophoretic Analysis ◽  
Water Soluble ◽  
Soluble Complex ◽  
Ph Values ◽  
Scattering Measurements ◽  
Water Soluble Complex

A water-soluble pigment excreted from Serratia marcescens has been purified by precipitation with ammonium sulphate, dialysis, and ultracentrifugation at different pH values. The purified pigment showed a single band in the ultracentrifuge and by electrophoretic analysis at several pH values. An average molecular weight of 5 × 106 was calculated from light-scattering measurements. This pigment is composed of carbohydrate and protein combined with prodigiosin, and several properties of the complex are described.

Assembly of Nanoparticles from Bioactive Peptides and Chitosan

2011 ◽  
Vol 1312 ◽  
Author(s):  
B. Hu ◽  
Q. R. Huang ◽  
X. X. Zeng
Keyword(s):  
Electrophoretic Mobility ◽  
Bioactive Peptides ◽  
Molecular Chain ◽  
Mass Ratio ◽  
Ph Values ◽  
Transmission Electron ◽  
Low Salt ◽  
Liquid Chromatography Tandem Mass ◽  
Positively Charged ◽  
Critical Ph

ABSTRACTAssembly of nanoparticles from bioactive peptides, caseinophosphopeptides (CPPs) and chitosan (CS) at physiological conditions and various CS/CPPs mass ratios have been systematically studied using a combination of turbidimetric titration, dynamic light scattering (DLS), electrophoretic mobility (zeta-potential) and transmission electron microscopy (TEM). Peptides, incorporated with CS forming nanoparticles, have already been prepared and identified using liquid chromatography-tandem mass spectrometry (LC-MS-MS). They are characteristic with different amount of clusters of phosphorylated seryl residues. At low salt concentration, an increase of CS/CPP mass ratio shifted the critical pHϕ1, which designated the formation of CS/CPP nanocomplexes, as well as pHmax, representing the neutralization of positive and negative charge to higher pH values. The peptide-polymer binding mechanism was analyzed according to the results of DLS, electrophoretic mobility, and TEM. First, negatively charged CPPs absorbed to positively charged CS molecular chain to form intrapolymer nanocomplexes saturated with CPPs (CPPNP). Then, the negatively charged CPPNP was bridged by added positively charged CS. Finally, novel nano-scaled spherical brushes were formed as additional CS molecule absorbed back to and bound the CPPNP. Phosphorylated groups in the CPPs might be the dominant sites for interaction with –NH3+ on the CS molecular chain.

Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins

1991 ◽  
Vol 58 (4) ◽  
pp. 461-467 ◽  
Author(s):  
Rosina López-Fandiño ◽  
Mercedes Ramos ◽  
Estrella Fernández-García ◽  
Agustin Olano
Keyword(s):  
Bacillus Subtilis ◽  
Electrophoretic Mobility ◽  
Proteolytic Activity ◽  
Aspergillus Oryzae ◽  
Electrophoretic Analysis ◽  
Breakdown Product ◽  
Commercial Enzymes ◽  
Fungal Protease ◽  
Hydrolysis Of

SummaryElectrophoretic analysis of the action of two commercial enzymes, Neutrase 0·5 and MKC Fungal Protease, on whole casein and αs-, β- and κ-caseins from cows' and ewes' milk showed that Neutrase 0·5 chiefly degraded β-casein, giving rise to peptides soluble at pH 4·6 detectable by PAGE. In contrast, although MKC Fungal Protease caused intense hydrolysis of bovine β-casein, in ovine casein it resulted in more active degradation of αs- than β-casein. The latter enzyme did not produce peptides soluble at pH 4·6 detectable by PAGE. Both enzymes degraded κ-casein, yielding a breakdown product that exhibited an electrophoretic mobility similar to that of the breakdown product produced by the action of commercial rennet.

Sign in / Sign up

Export Citation Format

Share Document