The Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.

scholarly journals Hemoglobin Hope: A Beta Chain Variant

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 830-838 ◽  
Author(s):  
VIRGINIA MINNICH ◽  
ROBERT J. HILL ◽  
PHILIP D. KHURI ◽  
MARY E. ANDERSON
Keyword(s):  
Blood Cells ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Beta Chain ◽  
Agar Gel ◽  
Hemoglobin A ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Agar Gel Electrophoresis ◽  
Chain Variant

Abstract A new hemoglobin, hemoglobin Hope, with a beta chain abnormality has been found in three generations of a St. Louis Negro family. The abnormal hemoglobin in the heterozygous state caused neither clinical stigmata nor abnormality in the red blood cells. Hemoglobin Hope was detected by agar gel electrophoresis at pH 6.2, but could not be differentiated from hemoglobin A by starch block electrophoresis at pH 8.6. Also, it could not be separated from hemoglobin A by paper, or starch gel electrophoresis employing a range of buffers from pH 6.2 to 8.6. Amino acid analysis showed that aspartic acid was substituted for glycine at position 136 of the beta chain. Hemoglobin Hope may be formulated as α2Aβ2136 gly-asp.

scholarly journals Electrophoretic Characterization of Taxus Cultivars

1993 ◽  
Vol 3 (4) ◽  
pp. 430-433
Author(s):  
C.E. Greer ◽  
R.E. Schutzki ◽  
A. Fernandez ◽  
J.F. Hancock
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

Starch gel electrophoresis was used to fingerprint 55 Taxus plants, listed as 21 species and/or cultivars. Plants were analyzed for six enzymes, representing eight putative loci. Within many of the cultivars, different fingerprints were observed, indicating nomenclatural errors in Taxus.

scholarly journals The Amino Acid Composition of Hemoglobin. III. A Qualitative Method for Identifying Abnormalities of the Polypeptide Chains of Hemoglobin

Blood ◽  
1964 ◽  
Vol 24 (6) ◽  
pp. 750-756 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON M. PETTIT
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Gel Electrophoresis ◽  
Qualitative Method ◽  
Polypeptide Chain ◽  
Starch Gel Electrophoresis ◽  
Simple Method ◽  
Starch Gel ◽  
Barbital Buffer ◽  
Polypeptide Chains

Abstract A relatively simple method is described which permits the identification of abnormalities of either polypeptide chain of hemoglobin. The procedure is based on the dissociation of hemoglobin by 6 molar urea and starch-gel electrophoresis in a barbital buffer at pH 8.0.

scholarly journals The Fractionation of ?-Histones From Chicken Erythrocyte Nuclei

1964 ◽  
Vol 17 (4) ◽  
pp. 1001 ◽  
Author(s):  
JT Bellair ◽  
OM Mauritzen
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Chicken Erythrocyte ◽  
Exclusion Chromatography ◽  
Starch Gel

Crude IX-histone, obtained from the original histone complex by precipitation of the f3-and y-histones with ethanol, has been shown by starch-gel electrophoresis to contain 13 components. The fractionation of IX-histone by exclusion chromatography on Sephadex G-200 is reported. While none of these components have been obtained pure in the present study, considerable purification of components 2, 3, 4, 5, 8, 9, 10, and 11 has been achieved, and their amino acid composition leaves no doubt that o::-histones represent a muoh larger family of "lysine-rich" proteins than was hitherto supposed.

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.

The tertiary phase of rennin action on αs- and β-caseins

1970 ◽  
Vol 37 (3) ◽  
pp. 437-444 ◽  
Author(s):  
A. M. El-Negoumy
Keyword(s):  
Amino Acid ◽  
Degradation Product ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Starch Gel Electrophoresis ◽  
Terminal Amino Acid ◽  
Starch Gel ◽  
Terminal Amino

SummaryCasein, whole αs-casein and β-casein were incubated for 3 and 14 h with crystalline rennin, at pH 6·60 and 36 °C, both in phosphate buffer and in milk dialysate. Products obtained from both systems, comprising 30–83% calciumsensitive (Cas) components, gave similar patterns on starch gel electrophoresis. Whole casein and whole αs-casein were not so soluble in milk dialysate as in phosphate buffer. No significant differences in composition were observed between the Cas and the calcium-insensitive (Ca1) products from the same source.The αs1-component of the Cas product from rennin-treated whole αs-casein had faster gel mobility in comparison to the αs1-component in the Cas product from untreated whole αs-casein. Also, αs1-casein yielded one faster-moving degradation product, while αs2,3,4 appeared unaltered after 14h. The Cas product of rennintreated β-casein also had faster mobility than untreated β-casein and yielded one faster degradation product and several minor ones of slower mobility. Arginine was the only N-terminal amino acid found in the Cas product of both rennin-treated and untreated αs - and β-caseins. The arginine content increased from 3·48 and 4·98 moles/105g to 5·12 and 6·38 moles/105g in the Cas products from rennin-treated β-and αs-caseins, respectively.

scholarly journals Investigation into the distribution and properties of histones and other basic proteins in bacteria

1966 ◽  
Vol 101 (3) ◽  
pp. 665-673 ◽  
Author(s):  
JL Leaver ◽  
HJ Cruft
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Starch Gel Electrophoresis ◽  
Basic Proteins ◽  
E Coli ◽  
Extraction And Purification ◽  
Starch Gel ◽  
Micro Organisms

1. Methods have been developed for the extraction and purification of bacterial basic proteins. These proteins were initially examined by a micro-method of starch-gel electrophoresis and were then characterized more fully. 2. Although it was found that most of the DNA in both Bacillus megaterium and Escherichia coli must be free from combination with basic protein, there was some evidence that a small portion might be in the form of a typical nucleohistone complex. 3. The ribosomes of both B. megaterium and E. coli were shown to contain approximately 2% of basic protein. On the basis of ultraviolet-absorption curves, partial amino acid analyses and their behaviour on electrophoresis in polyacrylamide gels, it was concluded that some of these ribosomal basic proteins may be extremely similar to typical histones. 4. These results are discussed in relation to those of other authors, and the possible functions of basic proteins present in micro-organisms are considered with reference to those that have already been proposed for the histones of higher organisms.

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