Occurrence of Major Whey Proteins in the pH 4.6 Insoluble Protein Fraction from UHT-Treated Milk

The effects of age and sulphur fertilization on various sulphur fractions in the legume Stylosanthes humilis were examined. Plant material was obtained in two consecutive seasons from nodulated plants growing in the field and from a glasshouse experiment. A very close relationship between the concentration of total nitrogen (Nt), that of total sulphur (St), and age was found. In young material Nt increased at first then reached a plateau with increases in St (brought about by additions of sulphur). As the plants aged, however, both Nt and St declined and the relation between them became more nearly linear. Nt and St were also closely related in seed from these plants but the St/Nt ratio was much lower than in the vegetative material. A moderate deficiency of sulphur had little effect on the ratio of alcohol-insoluble to total nitrogen. In contrast with published work on other species it was found that sulphur applications increased the ratio of sulphur to nitrogen in the alcohol-insoluble (protein) fraction.

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Synthesis of 2-amino-3-hydroxyacetophenone-0β-D-glucopyranoside : a fluorescent compound from insoluble protein fraction of aging human lens

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/s0960-894x(01)80333-4 ◽

1994 ◽

Vol 4 (10) ◽

pp. 1219-1220 ◽

Cited By ~ 1

Author(s):

Sanjoy Kumar Das ◽

Uttam Kumar Saha

Keyword(s):

Protein Fraction ◽

Human Lens ◽

Insoluble Protein ◽

Fluorescent Compound ◽

Insoluble Protein Fraction

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Direct Approach to Identification, at the Molecular Level, of Modified Proteins in Human Nuclear Cataractous Lenses: Beta-Crystallin is a Component of the Urea-Insoluble Protein Fraction

Ophthalmic Research ◽

10.1159/000267183 ◽

1992 ◽

Vol 24 (5) ◽

pp. 303-307 ◽

Cited By ~ 1

Author(s):

Richard A.J. O’Hair ◽

Margaret M. Sheil ◽

Roger J.W. Truscott

Keyword(s):

Protein Fraction ◽

Molecular Level ◽

Direct Approach ◽

Insoluble Protein ◽

Modified Proteins ◽

Insoluble Protein Fraction

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Variability of a water-insoluble protein fraction from maize pollen

Canadian Journal of Botany ◽

10.1139/b83-228 ◽

1983 ◽

Vol 61 (8) ◽

pp. 2119-2123 ◽

Cited By ~ 2

Author(s):

David K. Shortess

Keyword(s):

Protein Fraction ◽

Polyacrylamide Gel Electrophoresis ◽

Seed Proteins ◽

Solvent System ◽

Insoluble Protein ◽

Banding Patterns ◽

Maize Pollen ◽

System A ◽

High Level ◽

Insoluble Protein Fraction

An aqueous-insoluble protein fraction has been extracted from maize pollen using a solvent containing phenol, acetic acid, and water (2:1:1, w/v/v) in 3 M urea. The solvent extracted 26% of the total protein from the pollen. The proteins of this fraction were subjected to polyacrylamide gel electrophoresis using the same solvent system. A comparison of the banding patterns of 10 inbred lines and a commercial hybrid revealed a high level of variability among the lines. Some variability was also observed within lines. The degree of variability was similar to that observed in maize seed proteins extracted with the same solvent. However, a comparison of overall banding patterns and individual band intensity differences among the lines examined revealed no apparent homology between the proteins of the two tissues.

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Characterization of the insoluble protein fraction in the ocular lens

Canadian Journal of Biochemistry ◽

10.1139/o69-179 ◽

1969 ◽

Vol 47 (12) ◽

pp. 1115-1119 ◽

Cited By ~ 18

Author(s):

Sidney Lerman

Keyword(s):

Amino Acid ◽

Thin Layer ◽

Protein Fraction ◽

Human Lens ◽

Ocular Lens ◽

Insoluble Protein ◽

Alpha Crystallin ◽

Gamma Crystallin ◽

Insoluble Protein Fraction

The insoluble protein fraction of the ocular lens has been studied in four different species: the rat, dogfish, bovine, and human. These studies were performed in order to characterize the composition and formation of this protein in the ocular lens. On the basis of amino acid analyses, spectrophotometric determinations, thin-layer electrophoresis on Pevikon plates, and immunochemical data, it was concluded that in the rat and dogfish lens, the insoluble protein fraction derives mainly from the soluble gamma crystallin fraction. However, in the bovine and human lens, the insoluble protein fraction appears to derive mainly from the soluble alpha crystallin fraction.

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