Call Prefix : PR-T

Call Suffix : 1979

Call Cutter : T - AgCh 1

Location : SEARCA Library

Format : TD

Publisher : University of the Philippines Los Banos (UPLB),

Publication Date : September 1979

Publication Place : Philippines :

Summary : Defatted meal from ipil-ipil seeds was found to contain 34.40 not equal 0.13% crude protein. Total soluble proteins obtained by Osborne fractionation amounted to 79.79%. This is broken down as follows: 51.74% albumins, 13.95% globulins, 3.90% prolamins and 10.03% gluteins. The residue contained 11.92% proteins. All fractions except the prolamins were characterized for their physico-chemical properties. Solubility test showed that both albumins and globulins were least soluble at pH 7.0. When chromatographed through Sephadex G-150, albumins exhibited two peaks (MW = 243,700), globulins two peaks (MW = 236,000) and gluteins three peaks (MW = 100,500). Electrophoretic properties revealed eleven bands for albumins, eight bands for globulins and two bands for glutelins. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate resulted in eight zones for albumins (MW = 363,900), nine zones for globulins (MW = 368,000) and three zones for glutelins (MW = 114,500). Amino acid profile indicated the presence of all essential amino acids. However, the amounts of sulfur-containing amino acids and trytophan were lower than those corresponding to the FAO protein pattern.