Fractionation and amino acid analysis of the salt-soluble protein fractions of normal and high-lysine barleys

1980 ◽  
Vol 31 (5) ◽  
pp. 467-473 ◽  
Author(s):  
Anthony P. Rhodes ◽  
Anthony A. Gill
Keyword(s):  
Amino Acid ◽  
Soluble Protein ◽  
Amino Acid Analysis ◽  
Protein Fractions ◽  
High Lysine

SCREENING FOR HIGH-LYSINE CULTIVARS IN A BARLEY BREEDING PROGRAM

1976 ◽  
Vol 56 (4) ◽  
pp. 817-821 ◽  
Author(s):  
D. E. LABERGE ◽  
A. W. MACGREGOR ◽  
D. R. METCALFE
Keyword(s):  
Amino Acid ◽  
Normal Level ◽  
Amino Acid Analysis ◽  
Cereal Grains ◽  
High Lysine ◽  
Protein Levels ◽  
Hordeum Distichum ◽  
Barley Protein ◽  
Selection Of

The UDY dye-binding method for determining protein levels in cereal grains was applied to an F2 population derived from a cross between OR 585, a two-rowed selection of barley (Hordeum distichum L. emend Lam.) possessing the "Hiproly" gene(s) for high lysine and TR 412, a two-rowed selection with a normal level of lysine. Seed of the two parental gentoypes produce different UDY absorbance values at similar protein levels. If UDY absorbance values are determined for the parental genotypes over a range of barley protein contents, the different regression lines for OR 585 and TR 412 parental barleys can be used to segregate F2 progeny that express the gene for high lysine. Determination of lysine by the UDY method closely agrees with lysine values determined by amino acid analysis.

COMPARISON OF METHODS FOR LYSINE SCREENING IN BARLEY

1976 ◽  
Vol 56 (1) ◽  
pp. 25-30 ◽  
Author(s):  
D. E. LABERGE ◽  
R. TKACHUK ◽  
D. R. METCALFE
Keyword(s):  
Amino Acid ◽  
Soluble Protein ◽  
Binding Capacity ◽  
Water Soluble ◽  
Ground Sample ◽  
High Lysine ◽  
Water Soluble Protein ◽  
Amino Acid Analyzer ◽  
Dye Binding ◽  
Highly Correlated

Two more rapid colorimetric procedures for crude protein were compared with amino acid analyses of lysine on an amino acid analyzer. The methods were found to be useful and inexpensive compared with amino acid analyses for segregating high-lysine selections of barley (Hordeum sp.). UDY absorbance, which is related to the dye-binding capacity of basic amino acids, was highly correlated with lysine when expressed as milligrams of lysine per 100 mg of ground sample (r = −0.919). When lysine was expressed as grams of lysine per 100 g of protein, the correlation coefficient was −0.479. Low UDY absorbance (i.e., high dye-binding capacity) can be obtained from higher lysine level or higher protein content. Therefore, for more accurate analyses, a Kjeldahl determination should be performed on the samples. A highly significant correlation (r = 0.753) was observed for ninhydrin absorbance of aqueous extracts when compared with lysine analyses. Application of this method is based on the assumption that high-lysine proteins are in the water-soluble protein fractions. Since high ninhydrin absorbance may be produced by increased soluble protein containing normal levels of lysine, the lysine content of samples screened by this method should be verified by amino acid analyses.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

scholarly journals Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Zhongqi He ◽  
Christopher P. Mattison ◽  
Dunhua Zhang ◽  
Casey C. Grimm
Keyword(s):  
Mass Spectrometry ◽  
Soluble Protein ◽  
Extraction Efficiency ◽  
Storage Proteins ◽  
Protein Composition ◽  
Protein Fractions ◽  
Peptide Fragments ◽  
2S Albumin ◽  
Cottonseed Protein ◽  
Glandless Cottonseed

AbstractIn this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.

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