scholarly journals Starch-Gel Electrophoresis of Wheat Flour Proteins

1963 ◽  
Vol 16 (2) ◽  
pp. 342 ◽  
Author(s):  
Janet SD Graham
Keyword(s):  
Acetic Acid ◽  
Wheat Flour ◽  
Gel Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Similar Protein ◽  
Starch Gel ◽  
Protein Components ◽  
Electrophoresis Of Proteins

An improved apparatus and procedures for starch-gel electrophoresis of proteins of wheat flour are described; highly reproducible separation of the protein components was achieved. By starch-gel electrophoresis it was shown that similar protein components occur in the extracts of wheat flour obtained with a variety of solvents; however, there were marked differences in the proportions of these components in various extracts. Several protein components were present in the fJ'actions separated by ion-exchange chromatography of' the proteins soluble in Bodium pyrophosphate and of those soluble in acetic acid; some fractions containeda number of similar protein components.

scholarly journals N-acetyl-β-d-glucosaminidase in marmoset kidney, serum and urine

1978 ◽  
Vol 175 (3) ◽  
pp. 859-867 ◽  
Author(s):  
R J Pierce ◽  
R G Price ◽  
J S L Fowler
Keyword(s):  
Gel Electrophoresis ◽  
Human Liver ◽  
Deae Cellulose ◽  
Heat Stability ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Serum And Urine

N-Acetyl-beta-D-glucosaminidase activities were determined in homogenates of marmoset kidney, in serum and in urine by using the 4-methylumbelliferyl substrate. The enzyme activity was separated into several components by DEAE-cellulose ion-exchange chromatography, starch-gel electrophoresis and isoelectric focusing. The kidney contained two major forms of the enzyme, A and B, which had similar pH optima and Km values. The A-form bound to DEAE-cellulose at pH 6.8, migrated towards the anode on starch-gel electrophoresis and had a pI of 5.0. The B-form did not bind to DEAE-cellulose at pH 6.8, remained near the origin on starch-gel electrophoresis and had a pI of 7.64. The isoenzymes also differed in heat stability, the B-form being the more stable. Serum contained B-form activity and, in addition, two intermediate forms (I1 and I2) were loosely bound to DEAE-cellulose. The serum A-form activity was less firmly bound to DEAE-cellulose than was the tissue A-form and was designated As. Serum from a pregnant marmoset contained a form which may be analogous to the human P-isoenzyme. Urine contained only a small amount of B-form activity, the majority being present in the A-form. The kidney A- and B-forms both had mol.wts. of 96000–100000 and the activity was predominantly lysosomal. Partial purification of the kidney A isoenzyme was undertaken. Immunoprecipitation studies indicated a relationship between marmoset kidney A-form and human liver A-form activity.

scholarly journals Extensive Protein Similarity of the Hybridizing Chickadees Parus atricapillus and P. carolinensis

The Auk ◽  
1986 ◽  
Vol 103 (4) ◽  
pp. 667-675 ◽  
Author(s):  
Michael J. Braun ◽  
Mark B. Robbins
Keyword(s):  
Contact Zone ◽  
Gel Electrophoresis ◽  
Isozyme Variation ◽  
Starch Gel Electrophoresis ◽  
Parus Atricapillus ◽  
Parus Gambeli ◽  
Starch Gel ◽  
Well Differentiated ◽  
Emerging Pattern ◽  
Electrophoresis Of Proteins

Abstract Starch gel electrophoresis of proteins was used to assess genetic differentiation and introgression across a contact zone between Parus atricapillus and P. carolinensis. Little or no differentiation was found at 35 presumed genetic loci, even between distantly allopatric population samples. Nei's (1978) genetic distance (D) was ≤0.001 for all comparisons. In contrast, Parus gambeli, another chickadee known to hybridize with atricapillus, was well differentiated at 3 loci (D ≈ 0.065). While the data suggest that atricapillus and carolinensis are closely related, they do not allow conclusions on the extent of introgression across the contact zone. The implications of these data are discussed in the light of the emerging pattern of isozyme variation in birds.

scholarly journals The relationship between reversibility of fibril formation and subunit composition of rat skin collagen

1969 ◽  
Vol 113 (2) ◽  
pp. 419-422 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Fibril Formation ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Fractionation Procedure ◽  
Skin Collagen ◽  
Starch Gel ◽  
The Relationship

1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37°. On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.

Hemoglobin Mahidol: a new hemoglobin α-chain mutant

1970 ◽  
Vol 48 (9) ◽  
pp. 1066-1078 ◽  
Author(s):  
S. Pootrakul ◽  
G. H. Dixon
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Cyanogen Bromide ◽  
Starch Gel Electrophoresis ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Α Chain ◽  
Acid Alteration ◽  
Peptide Maps ◽  
Amino Acid Alteration

A slow (less anionic) hemoglobin mutant has been detected by starch gel electrophoresis of hemoglobin from three unrelated patients in Bangkok. Dissociation of the abnormal hemoglobin with p-hydroxymercuribenzoate showed that the α-chain was the site of the mutation. The mutant α-chain was isolated by carboxymethylcellulose chromatography in 8 M urea and 0.05 M β-mercaptoethanol. Peptide maps of trypsin and cyanogen bromide cleaved α-chain indicated that the amino acid alteration of the mutant was in the peptide corresponding to residues 62–76 of the α-chain. Further cleavage of this peptide with 0.25 M acetic acid at 110 °C showed that residue 74 was changed from an aspartyl to a histidyl residue, a mutation not previously described. It is proposed that this new hemoglobin α274His β2A be called hemoglobin Mahidol after Mahidol University in Bangkok. In one of the three patients showing hemoglobin Mahidol, interaction with α-thalassemia occurs and, in this patient, hemoglobin A is totally absent, being replaced by hemoglobin Mahidol together with some hemoglobin H (β4A).

scholarly journals Isolation and Characterization of Protein Bodies From Developing Wheat Endosperm

1963 ◽  
Vol 16 (2) ◽  
pp. 375 ◽  
Author(s):  
Janet SD Graham ◽  
RK Morton ◽  
JK Raison
Keyword(s):  
Electron Microscopy ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Separation And Purification ◽  
Isolation And Characterization ◽  
Dense Bodies ◽  
Starch Gel ◽  
Slow Moving ◽  
Protein Components

Procedures are described for separation and purification of electron-dense bodies previously observed in intact endosperm by electron microscopy. Isolated bodies consist largely of protein. By starch-gel electrophoresis, the bodies contain predominantly slow-moving protein components similf1l' to those found in acetic acid extracts of whole endosperm.

scholarly journals The separation and characterization of marmoset kidney β-d-galactosidase and β-d-glucosidase

1977 ◽  
Vol 167 (3) ◽  
pp. 765-773 ◽  
Author(s):  
R J Pierce ◽  
R G Price
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Lysosomal Fraction ◽  
Glucosidase Activity ◽  
Starch Gel

beta-D-Galactosidase and beta-D-glucosidase activities were determined in homogenates of marmoset kidney by using the appropriate 4-methylumbelliferyl glycoside, beta-D-Galactosidase activity was separated into two main components by ion-exchange chromatography on DEAE-cellulose, starch-gel electrophoresis, isoelectric focusing and gel filtration on Sephadex G-200. One form designated A had a pI of 5.1, was loosely bound to DEAE-cellulose at pH7.0, remained near the origin on starch-gel electrophoresis at pH 7.0 and had an apparent molecular weight of 160000. The second beta-D-galactosidase component, designated B, was associated with the total beta-D-glucosidase activity, had a pI of 4.3, was firmly bound to DEAE-cellulose, migrated rapidly towards the anode on starch-gel electrophoresis and had an apparent molecular weight of 50000. The optimum pH values of beta-D-galactosidase A and B were 4.5 and 6.0 respectively. beta-D-Galactosidase A was activated by 0.1 M-NaC1 but the activity of the B form was inhibited by 1 M-NaC1 at pH 4.5. beta-D-galactosidase had a bimodal distribution, the A form being recovered in the lysosomal fraction whereas the B form was present in the soluble fraction, as was the major portion of the beta-D-glucosidase activity. The lysosomal and soluble forms were further characterized by DEAE-cellulose chromatography.

A revision of the species of Porphyra (Rhodophyta: Bangiales) occurring in British Columbia and adjacent waters

1992 ◽  
Vol 70 (10) ◽  
pp. 2066-2075 ◽  
Author(s):  
Sandra C. Lindstrom ◽  
Kathleen M. Cole
Keyword(s):  
British Columbia ◽  
New Species ◽  
North Pacific ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Southeast Alaska ◽  
Starch Gel ◽  
One New Species ◽  
New Distribution ◽  
Electrophoresis Of Proteins

Starch gel electrophoresis of proteins of Porphyra species occurring in British Columbia and nearby areas has provided new data on species identities. One new species is described, Porphyra kurogii (formerly identified as North Pacific P. purpurea), and its eastern Pacific distribution limit is extended from northern to southern British Columbia. Porphyra maculosa is recognized to be a taxonomic synonym of P. fucicola; new distribution records are provided. Porphyra cuneiformis is the correct name for specimens formerly identified as P. miniata in the area, and P. occidentalis is the correct name for most local specimens of P. "variegata." A key to the 21 species and 2 subspecies of Porphyra currently recognized in Oregon, Washington, British Columbia, and southeast Alaska is provided. The key includes the recently described P. mumfordii, P. fallax ssp. fallax, and P. fallax ssp. conwayae. Key words: isozymes, key, Porphyra, taxonomy.

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