Zone electrophoresis of conarachin, α-conarachin and bovine serum albumin on polyacrylamide gel

Gel electrophoretic analysis of peanut proteins and enzymes. I. Characterization of DEAE-cellulose separated fractions

“…Most enzyme activity was found in the conarachin fraction (Fraction I + II + III) and was similar to that of the total extract. Some diffuse activity was associated with arachin but this may be simple adsorption of enzyme molecules to this globulin (Evans et al, 1962).…”

“…There have been many investigations on the reserve proteins of peanuts because of their potential usefulness as food supplements. In general, these studies have shown that most of the proteins are easily extractable (Altschul et al, 1961(Altschul et al, , 1964aDawson, 1971; Dechary and Altschul, 1966;Dechary et al, 1961) and can be separated into two major fractions, arachin and conarachin (Daussant et al, 1969a,b;Dechary et al, 1961; Evans et al, 1962;Neucere, 1969; Neucere and Ory, 1970). More extensive purification of these two fractions (Dawson, 1971;Evans et al, 1962;Tombs, 1965;Tombs and Lowe, 1967;Neucere, 1969) has revealed that they are composed of complex large molecular weight globulins (a-arachin, a-conarachin), plus some other closely related components, not completely separated by the usual techniques.…”

Effects of Heat Treatments on Peanut Arachin and Conarachin

“…Arachin and conarachin, two major globulins in peanut cotyledons, were fractionated and named by Johns and Jones (1916). Since then extensive studies and various procedures were applied for the preparation of these peanut globulins (Jones and Horn 1930;Johnson and Naismith 1953;Evans et al 1962;Shetty and Rao 1974;Basha and Cherry 1976;Yaniada et al 1979b). In this study, based on observations from the literature, a practical procedure to prepare arachin and conarachin was developed whereby phosphate buffer extracts (pH 7.9, 0.05 and 0.20 M ) were consecutively fractionated by ammonium sulfate with 40, 60 and 85% saturation (Fig.…”

Identification of methionine-rich polypeptides in peanut (Arachis hypogaea L.) seed

“…Limited exploratory research has shown that there are genotypes within the species hypogaea with a better balance of nutritionally important amino acids than that 0021-8561/81/1429-0331 $01.25/0 © 1981 American Chemical Society found in the commercial cultivars (Heinis, 1972;Young et al, 1973;Pancholy et al, 1978). Although the arachin and conarachin fractions have been subjected to numerous studies (Jones and Horn, 1930;Johnson and Shooter, 1950; Dechary et al, 1961;Evans et al, 1962;Dausant et al, 1969; Dawson, 1968; Shetty and Rao, 1974;Basha and Cherry, 1976; Neucere and Conkerton, 1978), very little information is available on their polypeptide composition and relative nutritional importance of individual polypeptides. Since, methionine is an essential amino acid and is deficient in peanuts, a study was initiated to identify and isolate the peanut polypeptides that are rich in methionine.…”