NATURE OF PROTEINS INTRITICALEAND ITS PARENTAL SPECIES: II. GEL FILTRATION AND DISC ELECTROPHORESIS RESULTS

1970 ◽  
Vol 50 (1) ◽  
pp. 15-24 ◽  
Author(s):  
C. H. CHEN ◽  
W. BUSHUK
Keyword(s):  
Spring Wheat ◽  
Parental Species ◽  
Acetic Acid Solution ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Hard Red Spring Wheat ◽  
Molecular Weights ◽  
Electrophoretic Patterns ◽  
Water Salt ◽  
Protein Components

The compositions and identity of protein components in the water, salt solution, 70% ethanol, and acetic acid solution extracts of the endosperm from one line of Triticale, its parents, and one cultivar of hard red spring wheat were investigated by gel filtration and disc electrophoresis. Albumins, globulins, and gliadins, as defined by their solubility, molecular weight, and electrophoretic mobility, were obtained by gel filtration on Bio-Gel P-150. Approximate molecular weights determined from elution volumes were 1 × 104to 3 × 1045 × 104to 9 × 104, and above 1.5 × 105for albumins and globulins, gliadins and glutenins, respectively. Each gel-filtration fraction contained several protein components as determined by disc electrophoresis. Quantitative distribution of fractions varied with species. For each fraction the amount for Triticale was intermediate between the amounts for the parental species. The gel-filtration spectrum for Triticale was similar to that for the hard red spring wheat. However, disc electrophoretic patterns for fractions obtained by gel filtration for the two species were quite different.

NATURE OF PROTEINS IN TRITICALE AND ITS PARENTAL SPECIES: III. A COMPARISON OF THEIR ELECTROPHORETIC PATTERNS

1970 ◽  
Vol 50 (1) ◽  
pp. 25-30 ◽  
Author(s):  
C. H. CHEN ◽  
W. BUSHUK
Keyword(s):  
Durum Wheat ◽  
Spring Wheat ◽  
Interspecific Hybrid ◽  
Parental Species ◽  
Quality Factors ◽  
D Genome ◽  
Hard Red Spring Wheat ◽  
Electrophoretic Patterns ◽  
The Difference ◽  
Protein Components

Comparison of the disc electrophoretic patterns for the albumins, globulins, gliadins, and glutenins of one line of Triticale and its durum wheat and rye parents showed that all the protein components of the interspecific hybrid are present in the parents. It is concluded that the proteins of Triticale are simply inherited from its parents. The patterns for the albumin and globulin groups for the cultivar of durum wheal (Stewart 63) and the cultivar of hard red spring wheat (Manitou) investigated were identical. Differences were observed in the patterns for the gliadins and glutenins of these two wheats. These qualitative differences might account for the difference in their breadmaking qualities, and provide additional evidence in support of the hypothesis that the genes for breadmaking quality factors are in the D genome.

scholarly journals Purification and properties of α-galactosidases from Vicia faba seeds

1969 ◽  
Vol 113 (1) ◽  
pp. 49-55 ◽  
Author(s):  
P. M. Dey ◽  
J. B. Pridham
Keyword(s):  
Amino Acid ◽  
Vicia Faba ◽  
Aromatic Amino Acid ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Thermal Stabilities ◽  
Molecular Weights ◽  
Purification And Properties ◽  
Enzyme I ◽  
Carbohydrate Contents

Two forms of α-galactosidase, I and II, exist in Vicia faba seeds and these have been purified 3660- and 337-fold respectively. They behaved as homogeneous preparations when examined by ultracentrifugation, disc electrophoresis and gel filtration. The apparent molecular weights of enzymes I and II, as determined by gel filtration, were 209000 and 38000 respectively. The carbohydrate contents of enzymes I and II were 25% and 2·8% respectively, and the enzymes differed in their aromatic amino acid compositions. Enzyme I was split into six inactive subunits in the presence of 6m-urea. α-Galactosidases I and II showed different pH optima and Km and Vmax. values with p-nitrophenyl α-d-galactoside and raffinose as substrates, and also differed in their thermal stabilities.

ISOLATION OF LH, FSH AND TSH FROM HUMAN PITUITARIES AFTER THE REMOVAL OF HGH

1974 ◽  
Vol 77 (3) ◽  
pp. 485-497 ◽  
Author(s):  
P. A. Torjesen ◽  
T. Sand ◽  
N. Norman ◽  
O. Trygstad ◽  
I. Foss
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Disc Electrophoresis ◽  
Exchange Chromatography ◽  
Polyacrylamide Gel ◽  
Molecular Weights ◽  
Pituitary Glands

ABSTRACT Highly purified human LH, FSH and TSH were isolated from batches of 300 frozen pituitary glands (200 g) by pH, acetone and ethanol fractionation, Sephadex gel filtration, ion-exchange chromatography on DEAE-cellulose and CM-Sephadex, and preparative polyacrylamide-gel electrophoresis. Sodium dodecyl-sulphate (SDS) polyacrylamide gel electrophoresis was used in order to check the purity, the identity and the molecular weight of the purified LH, FSH and TSH. This procedure showed that the hormone preparations consisted of two subunits with molecular weights of: LH: 21 300 and 17 900, FSH: 22 100 and 18 300 and TSH: 20 800 and 16 400. The purity of the hormone preparations was also evaluated by analytical disc electrophoresis at pH 8.9. The purified hormone preparations had radioimmunological activity as follows: LH: 20 000 IU/mg, FSH: 16 500 IU/mg and TSH: 5 IU/mg. All preparations had high biological potency.

Changes in proteins of Domiati cheese during pickling

1972 ◽  
Vol 39 (2) ◽  
pp. 219-225 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
Safinaz El-Shibiny
Keyword(s):  
Amino Acids ◽  
Room Temperature ◽  
Gel Filtration ◽  
Electrophoretic Pattern ◽  
Pasteurized Milk ◽  
Molecular Weights ◽  
Electrophoretic Patterns ◽  
Related Substances ◽  
Nitrogenous Substances

SummaryDomiati cheese from homogenized and unhomogenized pasteurized milk was pickled for 4 months at room temperature. During pickling, the soluble tyrosine and tryptophan contents of the cheese gradually increased, indicating progressive proteolysis.Gel filtration of cheese extract on Sephadex G-25 revealed the presence of nitrogenous substances of various molecular weights. The maximum formation of amino acids and related substances was observed after 15 days storage.The changes in the electrophoretic patterns of proteins in the cheese during pickling indicated that both αs - and β-caseins were attacked. β-Casein, however, was much less affected.Homogenization was found to affect the formation of soluble nitrogenous substances, but was without effect on the electrophoretic pattern of the protein in the cheese.

scholarly journals MURINE AMYLOID FIBRIL PROTEIN: ISOLATION, PURIFICATION AND CHARACTERIZATION

1971 ◽  
Vol 19 (1) ◽  
pp. 16-28 ◽  
Author(s):  
G. G. GLENNER ◽  
D. PAGE ◽  
C. ISERSKY ◽  
M. HARADA ◽  
P. CUATRECASAS ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Structure Identification ◽  
Major Protein ◽  
Amyloid Protein ◽  
Molecular Weights ◽  
Sepharose 4B

Murine amyloid has been produced by four different induction methods ( Mycobacterium butyricum, casein, casein plus Freund's adjuvant and endotoxin-induced mouse amyloidosis) in several strains and obtained from mice with "spontaneous" amyloidosis. The amyloid fibrils have been concentrated from spleen and liver. Electron microscopy of all of these preparations reveals the amyloid fibril to be 100 Å in width and composed of two parallel filaments, each measuring 35-40 Å in width and having the appearance of a twisted ribbon. X-ray diffraction of all preparations reveals a "backbone" spacing at 4.75 Å and a "side chain" spacing at 11 Å indicating a "β-pleated sheet" structure. Identification of the major protein component of amyloid fibril concentrates was made by combined use of sodium dodecyl sulfate polyacrylamide disc electrophoresis, labeling of the protein with 3H-tryptophan and Sepharose 4B gel filtration. Purification of the amyloid protein from spontaneous amyloidosis liver was accomplished by sequential gel filtration with 5 M guanidine in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns. The material is a unique glycoprotein with a molecular weight of 7200, a high content of dicarboxylic and short chain amino acids, a significant amount of tryptophan and an unreactive NH2-terminal amino acid, tentatively identified as pyrrolid-2-one-5-carboxylic acid. There are no methionine, half-cystine, hydroxylysine or hydroxyproline residues. Murine amyloid protein, therefore, has striking similarities to many human amyloid protein preparations. It differs from the human proteins in the similarity of molecular weights of different preparations.

scholarly journals The purification and properties of a ribonucleoenzyme, o-diphenol oxidase, from potatoes

1970 ◽  
Vol 118 (1) ◽  
pp. 15-23 ◽  
Author(s):  
K. Balasingam ◽  
W. Ferdinand
Keyword(s):  
Molecular Weight ◽  
Specific Activity ◽  
Gel Filtration ◽  
High Specific Activity ◽  
Disc Electrophoresis ◽  
Ph Optimum ◽  
Molecular Weights ◽  
Major Form ◽  
Purification And Properties ◽  
Minimal Molecular Weight

1. o-Diphenol oxidase was isolated from potato tubers by a new approach that avoids the browning due to autoxidation. 2. There are at least three forms of the enzyme, of different molecular weights. The major form, of highest molecular weight, was separated from the others in good yield and with high specific activity by gel filtration through Bio-Gel P-300. 3. The major form is homogeneous by disc electrophoresis but regenerates small amounts of the species of lower molecular weight, as shown by rechromatography on Bio-Gel P-300. 4. There is an equal amount of RNA and protein by weight in the fully active enzyme. The RNA cannot be removed without loss of activity, and is not attacked by ribonuclease. 5. The pH optimum of the enzyme is at pH5.0 when assayed with 4-methylcatechol as substrate. It is ten times more active with this substrate than with chlorogenic acid or catechol. The enzyme is fully active in 4m-urea. 6. A minimal molecular weight of 36000 is indicated by copper content and amino acid analysis of the protein component of the enzyme. 7. The protein contains five half-cystinyl residues per 36000 daltons, a value similar to that found in o-diphenol oxidase from mushrooms. It also contains tyrosine residues although, when pure, it does not turn brown by autoxidation.

Studies on the purification of Entamoeba histolytica antigens by gel filtration. I. Some physicochemical properties of the isolated fractions

1970 ◽  
Vol 16 (6) ◽  
pp. 485-492 ◽  
Author(s):  
Z. Ali Khan ◽  
E. Meerovitch
Keyword(s):  
Physicochemical Properties ◽  
Entamoeba Histolytica ◽  
Isoelectric Focusing ◽  
Phosphate Buffer ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Aqueous Extracts ◽  
Molecular Weights ◽  
Isoelectric Ph ◽  
Considerable Loss

Aqueous extracts, prepared from Entamoeba histolytica (DKB strain) grown at 37 °C in TTY medium with Crithidia sp., were chromatographed on Sephadex G-200 and G-100 gels equilibrated with 0.15 M phosphate buffer, pH 7.2. Seven fractions were obtained, the molecular weights of which ranged from 650 000 to [Formula: see text]. The absorption spectra of either the whole amoebic extract or the first two fractions from the G-200 column were in the region of 280 mμ. The protein to carbohydrate ratio of the whole undialyzed amoebic extract was 2.6:1, which changed to 17:1 after dialysis, indicating a considerable loss of carbohydrate. The whole amoebic extract when subjected to disc electrophoresis resolved into 26 protein bands while the fractions, in addition to having contaminants from the preceding peaks, also contained their own characteristic protein bands. The first two fractions contained, as determined by disc electrophoresis and isoelectric focusing, a variety of different anionic proteins. The isoelectric pH of the first fraction was 5.8 to 6.0 and that of the second ranged between 4.5 and 6.4.

Anticoagulants Produced by Thrombin from Fibrin, the Effect on Blood Coagulation, Some Physical Characteristics

1971 ◽  
Vol 26 (02) ◽  
pp. 211-223 ◽  
Author(s):  
Ch R. Muirhead ◽  
D. C Triantaphyllopoulos
Keyword(s):  
Blood Coagulation ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Fibrin Clot ◽  
Disc Electrophoresis ◽  
Physical Characteristics ◽  
Advanced Stage ◽  
Kallikrein Inhibitor ◽  
Shed Blood ◽  
Complete Lysis

SummaryChromatographed thrombin in the presence of both 50 Kallikrein inhibitor units of Trasylol per ml and 0.1 M E-ACA solubilized fibrin and the products of lysis possessed anticoagulant properties. The peak of the antithrombic activity coincided with the time of complete lysis of the fibrin clot, plasmin lysed fibrin exhibited the peak of its antithrombic activity much earlier. The effect of thrombin lysed fibrin on the prothrombin consumption of shed blood was found to be inhibitory.The products of the digestion of fibrin by thrombin and by plasmin, isolated at an advanced stage of proteolysis were compared by gel filtration, disc electrophoresis and DEAE cellulose chromatography. Differences in physical characteristics of these fibrin breakdown products offer evidence that they were produced by two different enzymes.

Registration of ‘Duclair’ Hard Red Spring Wheat

2011 ◽  
Vol 5 (3) ◽  
pp. 349-352 ◽  
Author(s):  
S. P. Lanning ◽  
G. R. Carlson ◽  
P. F. Lamb ◽  
D. Nash ◽  
D. M. Wichman ◽  
...  
Keyword(s):  
Spring Wheat ◽  
Hard Red Spring Wheat

Hybrid Vigor in Hard Red Spring Wheat Crosses 1

Crop Science ◽  
1970 ◽  
Vol 10 (3) ◽  
pp. 220-223 ◽  
Author(s):  
Darrell. G. Wells ◽  
Charles L. Lay
Keyword(s):  
Spring Wheat ◽  
Hybrid Vigor ◽  
Hard Red Spring Wheat
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