FRACTIONATION OF NITROGEN IN DEVELOPING WHEAT KERNELS

1938 ◽  
Vol 16c (7) ◽  
pp. 263-273 ◽  
Author(s):  
A. G. McCalla
Keyword(s):  
Soluble Protein ◽  
Chemical Nature ◽  
Water Soluble ◽  
Protein Fractions ◽  
Kernel Development ◽  
Protein Nitrogen ◽  
Wheat Kernel ◽  
Water Soluble Protein ◽  
Main Portion ◽  
Wheat Kernels

Total nitrogen in developing wheat kernels was fractionated to give non-protein nitrogen and three protein fractions. Each fraction was hydrolyzed and analyzed for amide and arginine nitrogen.All fractions increased in amide and decreased in arginine nitrogen during kernel development. The main portion of the water-soluble protein is static in nature, and is considered to play no part in the metabolism of the endosperm proteins. The trend, with time, of amide in the two other protein fractions (soluble and insoluble in normal potassium iodide) was closely parallel to the trend of amide in non-protein nitrogen. The chemical nature of each of the gluten fractions in flour from the most insoluble to the most soluble is determined by the chemical nature of successive portions of the non-protein nitrogen in the wheat kernel at progressive stages of maturity.

BIOCHEMICAL CHANGES IN SHRIMP INOCULATED WITH PSEUDOMONAS, BACILLUS AND A CORYNEFORM BACTERIUM1,2

1971 ◽  
Vol 34 (11) ◽  
pp. 533-547 ◽  
Author(s):  
B. F. Cobb ◽  
C. Vanderzant
Keyword(s):  
Soluble Protein ◽  
Water Soluble ◽  
White Shrimp ◽  
Total Volatile ◽  
Protein Nitrogen ◽  
Fluorescent Pseudomonas ◽  
Water Soluble Protein ◽  
Penaeus Setiferus ◽  
Pseudomonas Species ◽  
Reducing Substances

White shrimp (Penaeus setiferus) washed with ethanol and sterile water were inoculated with a fluorescent Pseudomonas, non-fluorescent Pseudomonas, Bacillus, and a coryneform bacterium. Washing reduced the microbial load but growth occurred on control samples during refrigerated storage. Samples inoculated with Pseudomonas became putrid 2–3 days sooner than their controls. Addition of coryneform bacteria delayed spoilage. Shrimp inoculated with Bacillus spoiled at the same time as the non-inoculated controls. Inoculation of shrimp with Pseudomonas species (a) retarded development of melanosis; (b) produced volatile nitrogen in the atmosphere surrounding shrimp but only after spoilage had taken place; (c) caused higher levels of water-soluble protein, non-protein nitrogen, and total volatile nitrogen than in their corresponding controls; and (d) reached higher pH levels sooner than the controls. No significant changes occurred in volatile reducing substances. Sterile shrimp juices exhibited more extensive melanosis than juices inoculated with Pseudomonas. No marked changes in amounts of soluble protein or non-protein nitrogen were noted upon storage of inoculated juices. Juices inoculated with Pseudomonas had higher levels of total volatile nitrogen after storage than comparable controls. Proteolysis by the fluorescent Pseudomonas was indicated by major changes in elution profiles on Sephadex G-100. Compared with sterile controls, levels of free amino acids decreased in juices inoculated with Pseudomonas or Bacillus and stored at 5 C.

A trypsin inhibitor from the water-soluble protein fraction of wheat kernel

1989 ◽  
Vol 28 (5) ◽  
pp. 1307-1311 ◽  
Author(s):  
Elia Poerio ◽  
Lucia Carrano ◽  
Anna Maria Garzillo ◽  
Vincenzo Buonocore
Keyword(s):  
Trypsin Inhibitor ◽  
Soluble Protein ◽  
Protein Fraction ◽  
Water Soluble ◽  
Soluble Protein Fraction ◽  
Wheat Kernel ◽  
Water Soluble Protein

THE SOLUBLE PROTEINS OF THE MUSCLE TISSUE OF THE HADDOCK

1931 ◽  
Vol 6 (1) ◽  
pp. 1-11 ◽  
Author(s):  
J. F. LOGAN
Keyword(s):  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Muscle Tissue ◽  
Soluble Protein ◽  
Potassium Phosphate ◽  
Extraction Methods ◽  
Water Soluble ◽  
Tabular Form ◽  
Water Soluble Protein ◽  
Isoelectric Points

As a contribution to the chemistry of muscle tissue, the solubility of the protein of haddock muscle in aqueous solutions of sodium chloride and neutral potassium phosphate, respectively, was determined. The results are expressed in tabular form and graphically in the form of solubility curves. A water-soluble protein and also a salt-soluble protein were isolated from dialyzed haddock muscle by extraction methods. These proteins were obtained in a comparatively pure condition by precipitation from solution in the region of their isoelectric points.

FRACTIONATION OF LIVETIN AND THE MOLECULAR WEIGHTS OF THE α- AND β-COMPONENTS

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook
Keyword(s):  
Light Scattering ◽  
Soluble Protein ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Water Soluble ◽  
Water Soluble Fraction ◽  
Molecular Weights ◽  
Water Soluble Protein ◽  
Hen Egg Yolk ◽  
Hen Egg

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.

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