A comparative study of the insoluble storage proteins and the lectins of seeds of the Euphorbiaceae

1984 ◽  
Vol 62 (8) ◽  
pp. 1671-1677 ◽  
Author(s):  
Louise Lalonde ◽  
David W. Fountain ◽  
Allison Kermode ◽  
Francis B. Ouellette ◽  
Kelly Scott ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Castor Bean ◽  
Storage Proteins ◽  
Reduced Form ◽  
Polyacrylamide Gels ◽  
Salt Solutions ◽  
Sodium Dodecylsulphate ◽  
Molecular Weight Range ◽  
Jatropha Gossypifolia ◽  
Major Storage Protein

The major storage protein within seeds of the Euphorbiaceae is the 11S crystalloid, which is only completely soluble in buffer or salt solutions if sodium dodecylsulphate or urea is present. Prior to this study, only the storage proteins of the castor bean had been characterized. The nonreduced crystalloid protein complex in all species tested has a molecular weight of 50 000 – 55 000, and in reduced form the proteins migrate on polyacrylamide gels as two distinct groups of polypeptides, one in the molecular weight range 20 000 – 25 000 and the other in the 29 000 – 35 000 range. In this respect the proteins have the general characteristics of those of castor bean, but only the proteins of Jatropha gossypifolia show striking similarities. Within any one genus, the storage proteins appear to be more or less identical (e.g., Manihot spp.) or show distinct differences (e.g., Euphorbia spp.). The soluble lectin proteins of J. gossypifolia have very similar haemagglutination properties to those of castor bean lectins, and the glycoproteins of both species separate similarly on polyacrylamide gels. Few other species contain glycoproteins or lectins that can cause agglutination.

An electrophoretic analysis of the seed proteins from Pinus monticola and eight other species of pine

1988 ◽  
Vol 66 (9) ◽  
pp. 1808-1812 ◽  
Author(s):  
David J. Gifford
Keyword(s):  
Molecular Mass ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Sodium Dodecyl ◽  
Reduced Form ◽  
Major Protein ◽  
Polyacrylamide Gels ◽  
Pinus Monticola ◽  
Embryonic Axes ◽  
Pinus Species

The major storage proteins of mature Pinus monticola Dougl. seed megagametophytes are crystalloids and are only completely soluble in buffer solutions if sodium dodecyl sulphate is present. These insoluble proteins-constitute 50% of the storage reserve in the seed. Crystalloid proteins are found in embryonic axes also and are a major protein reserve in mature seeds from all other Pinus species examined. These proteins in their nonreduced form have molecular masses of 51 – 55 kilodaltons (kDa) and in reduced form migrate on polyacrylamide gels as two distinct groups of proteins, one in the molecular mass range 31 – 34.5 kDa and the other in the 21.5 – 22.5 kDa range. The pine crystalloid proteins are not glycosylated and have similar solubility, structural, and size characteristics to crystalloid proteins found in other seed types, such as Ricinus communis and Cucurbita species. However, they are immunologically different from the crystalloid proteins of R. communis. In general, the soluble protein gel profiles vary considerably among the species. Some similarities do exist; in particular, a group of proteins in the 27 – 29.5 kDa molecular mass regions of polyacrylamide gels is common to all Pinus species examined. The soluble proteins are not glycosylated.

Soluble Fibrin Complexes and Fibrinogen Heterogeneity in Diabetes mellitus

1980 ◽  
Vol 44 (03) ◽  
pp. 130-134 ◽  
Author(s):  
E B Tsianos ◽  
N E Stathakis
Keyword(s):  
Diabetes Mellitus ◽  
Molecular Weight ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Polyacrylamide Gels ◽  
Soluble Fibrin ◽  
Α2 Macroglobulin ◽  
Patients With Diabetes

SummaryThe presence of soluble fibrin complexes (SFC) measured by gel filtration of plasma on 4% agarose columns, fibrinogen heterogeneity on 3.5% SDS-polyacrylamide gels and the concentrations of several plasma proteins were evaluated in 39 patients with diabetes mellitus (DM) and 19 matched control subjects. A small but significant increase of SFC was found in DM (p<0.01). On individual basis 51.2% of the patients had increased SFC (>M + 2 SD of the controls). Polyacrylamide gel electrophoresis of the SFC showed no evidence of cross-linking or proteolysis. Plasma clots formed in the presence of EDTA and trasylol were analysed in SDS-polyacrylamide gels in a normal and two lower molecular weight fibrin bands (band I, II, III). The percentage of band I fibrinogen was in diabetics (65.3 ± 4.7%) lower than that of the controls (71.8 ± 4.5%) (p < 0.01). Fibrinogen levels, antithrombin III, α1-antitrypsin, α2-macroglobulin and plasminogen were significantly increased in DM. We suggest that in DM there is an enhancement of intravascular fibrin formation and accelerated fibrinogen degradation to lower molecular weight forms.

scholarly journals Nuclear matrix of HeLa S3 cells. Polypeptide composition during adenovirus infection and in phases of the cell cycle.

1977 ◽  
Vol 72 (1) ◽  
pp. 194-208 ◽  
Author(s):  
L D Hodge ◽  
P Mancini ◽  
F M Davis ◽  
P Heywood
Keyword(s):  
Cell Cycle ◽  
Molecular Weight ◽  
Nuclear Matrix ◽  
Apparent Molecular Weight ◽  
Molecular Weight Range ◽  
Weight Range ◽  
Molecular Weights ◽  
Liver Nuclei ◽  
Hela S3 ◽  
Biochemical Analyses

A subnuclear fraction has been isolated from HeLa S3 nuclei after treatment with high salt buffer, deoxyribonuclease, and dithiothreitol. This fraction retains the approximate size and shape of nuclei and resembles the nuclear matrix recently isolated from rat liver nuclei. Ultrastructural and biochemical analyses indicate that this structure consists of nonmembranous elements as well as some membranous elements. Its chemical composition is 87% protein, 12% phospholipid, 1% DNA, and 0.1% RNA by weight. The protein constituents are resolved in SDS-polyacrylamide slab gels into 30-35 distinguishable bands in the apparent molecular weight range of 14,000 - 200,000 with major peptides at 14,000 - 18,000 and 45,000 - 75,000. Analysis of newly synthesized polypeptides by cylindrical gel electrophoresis reveals another cluster in the 90,000-130,000 molecular weight range. Infection with adenovirus results in an altered polypeptide profile. Additional polypeptides with apparent molecular weights of 21,000, 23,000, and 92,000 become major components by 22 h after infection. Concomitantly, some peptides in the 45,000-75,000 mol wt range become less prominent. In synchronized cells the relative staining capacity of the six bands in the 45,000-75,000 mol wt range changes during the cell cycle. Synthesis of at least some matrix polypeptides occures in all phases of the cell cycle, although there is decreased synthesis in late S/G2. In the absence of protein synthesis after cell division, at least some polypeptides in the 45,000-75,000 mol wt range survive nuclear dispersal and subsequent reformation during mitosis. The possible significance of this subnuclear structure with regard to structure-function relationships within the nucleus during virus replication and during the life cycle of the cell is discussed.

Structure and Solution Properties of High Molecular Weight Butadiene-Styrene Copolymers

1957 ◽  
Vol 30 (1) ◽  
pp. 315-325
Author(s):  
R. B. MacFarlane ◽  
L. A. McLeod
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Complex Structure ◽  
Mixed Solvents ◽  
Solution Time ◽  
Solution Viscosity ◽  
Solution Properties ◽  
Molecular Weight Range ◽  
Viscosity Measurements ◽  
Commercial Practice

Abstract Production of high molecular weight copolymers of butadiene and styrene for use in oil-extended rubbers has aroused interest in the solution properties of copolymers above the molecular weight range commonly encountered in commercial practice. It has been observed that solubility of such polymers in toluene is a time-dependent phenomenon and the apparent solubility can increase continuously, in the absence of agitation, for as long as 800 hours. Although a standard Harris cage solubility test may show the presence of 50% gel, other properties do not confirm the presence of any appreciable quantities of insoluble material. Mild agitation rapidly promotes almost complete solubility. Dilute solution viscosity measurements are very misleading unless the influence of solution time is recognized and apparent intrinsic viscosities rise progressively with time of contact of the sample with solvent. This time-dependence of solution has been found to occur at conversions higher than 50% and is also a function of the amount of modifier used in the polymerization recipe. It has not been possible to shorten the solution time for viscosity measurements by mild heating or gentle agitation. Mixed solvents cause a change in the amount of increase of the apparent intrinsic viscosity but do not shorten the time to equilibrium. Measurement of the slope constant in the Huggins viscosity equation indicate that these solubility and viscosity effects coincide with the appearance of a marked degree of branching in the polymer molecules. The effect is, therefore, interpreted as being caused by the relatively slow disentanglement of molecules of complex structure.

Calcium-binding proteins in a vorticellid contractile organelle

1975 ◽  
Vol 19 (1) ◽  
pp. 203-213
Author(s):  
W.B. Amos ◽  
L.M. Routledge ◽  
F.F. Yew
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Sodium Dodecyl ◽  
Aromatic Amino Acids ◽  
Calcium Binding Proteins ◽  
Polyacrylamide Gels ◽  
Protein Species ◽  
Low Concentrations

The proteins of the contractile spasmoneme of Zoothamnium have been examined for comparison with other motile systems. Though capable of calcium-induced contraction, glycerinated preparations of the spasmoneme contain neither actin nor tubulin at levels that can be detected in polyacrylamide gels. Sixty per cent of the protein in sodium dodecyl sulphate gels migrates in a band at a molecular weight of approximately 20,000, consisting largely of 2 similar protein species which are here given the name of spasmins. The amino acid composition of 2 spasmin fractions has been determined by a fluorimetric method. They are rich in Asx, Glx and serine, but have few aromatic amino acids and no cystine or methionine. In calcium-buffered polyacrylamide gels, it was observed that a reduction in the electrophoretic mobility of the spasmins was induced specifically by calcium (but not magnesium) at the same low concentrations as induce contraction. This indicates that the spasmins are calcium-binding proteins which may be involved directly in the calcium-induced contraction of the spasmoneme.

Variation in the electrophoretic band pattern of tuber proteins from somaclones of potato

1986 ◽  
Vol 106 (2) ◽  
pp. 427-428 ◽  
Author(s):  
D. B. Smith
Keyword(s):  
Molecular Weight ◽  
Band Pattern ◽  
Polyacrylamide Gels ◽  
Potato Varieties ◽  
Electrophoretic Band ◽  
Native Proteins ◽  
Solatium Tuberosum ◽  
Specific Variation

The soluble tuber proteins of potato (Solatium tuberosum) may be separated by electrophoresis on the basis of charge or molecular weight (Stegemann & Schnick, 1982; Maier & Wagner, 1981: Park et al. 1983). Considerable cultivar specific variation exists in the band patterns of these proteins and separation of native proteins in 6% polyacrylamide gels at pH 7·9 has been used as the basis of characterizing cultivars for the Index of European Potato Varieties (Stegemann & Schnick, 1982).

Uremic Neurotoxin in the Middle Molecular Weight Range

1980 ◽  
Vol 4 (2) ◽  
pp. 116-120 ◽  
Author(s):  
N.K. Man ◽  
G. Cueille ◽  
J. Zingraff ◽  
J. Boudet ◽  
A. Sausse ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Molecular Weight Range ◽  
Weight Range

scholarly journals Transformation-deficient mutants of Bacillus subtilis impaired in competence-specific nuclease activities

1982 ◽  
Vol 152 (1) ◽  
pp. 166-174
Author(s):  
J A Mulder ◽  
G Venema
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Magnesium Ions ◽  
Polyacrylamide Gels ◽  
Wild Type ◽  
Molecular Weights ◽  
Defective Mutant ◽  
Mutant Strains

A comparison of the nucleolytic activities in competent and physiologically low-competent wild-type cultures of Bacillus subtilis in DNA-containing sodium dodecyl sulfate-polyacrylamide gels revealed the existence of three competence-associated nuclease activities with apparent molecular weights of 13,000, 15,000, and 26,000. The three activities, which were dependent on manganese or magnesium ions, were specifically present in the competent fraction of a competent culture. The competence-associated nucleolytic activities of eight transformation-defective mutant strains were assayed, resulting in the following three classes of mutants: (i) four strains which, according to this assay, were not impaired in any of the nucleolytic activities mentioned above; (ii) one strain which was strongly impaired in the 13,000- and 26,000-molecular-weight activities, but showed a considerable level of the 15,000-molecular-weight activity; and (iii) three strains which were severely impaired in all three activities. The results indicated that the 26,000-molecular-weight activity was a dimer of the 13,000-molecular-weight activity and that this nuclease was involved in the entry of DNA.

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