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Seed globulins of Cajanus cajan

Qualitas Plantarum Plant Foods for Human Nutrition, 1977
Seed globulins ofCajanus cajan a widely cultivated legume were purified and characterised. About 78% of the seed proteins were salt soluble, out of which 61% were globulins which were further separated into three fractions. The ∞ fraction was insoluble at pH 4.7 and consisted of two subfractions. Fraction β and γ were soluble at pH 4.7.
T. Gopala Krishna   +2 more
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Hydrogen Ion Equilibria of Cajanus cajan Lectin

Journal of Protein Chemistry, 1998
Hydrogen ion titration of an affinity-purified mannose/glucose-specific lectin from Cajanus cajan pulse was carried out at 30 degrees C and ionic strength of 0.15 by a discontinuous method. The titration was reversible in the pH range 2-12.0. The numbers of different ionizable groups per 39,000 g of the lectin were 43 carboxyl groups (pKint = 3.93), 10
A, Salahuddin, R H, Khan
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Amylase inhibitors of pigeonpea (Cajanus cajan) seeds

Phytochemistry, 1998
Pigeonpea (Cajanus cajan L) seeds were analysed quantitatively for amylase inhibitor (AI) activity and qualitatively, by an in-gel-detection method on polyacrylamide gels. At least four AI isoforms were identified in pigeonpea seeds. The AIs inhibit human salivary and bovine pancreatic amylase but fail to inhibit bacterial, fungal and endogenous ...
A P, Giri, M S, Kachole
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Arabinans from Cajanus cajan cotyledon

Phytochemistry, 1991
Two arabinans were isolated in pure form, from the water-soluble extract of red gram cotyledons. Their structures were determined by a combination of methods including GC-MS and NMR. Both the arabinans were highly branched, with a backbone of a+arabinose units joined by 1+5 linkages and branched through O-2 and/or O-+3 linkage.
N.R. Swamy, P.V. Salimath
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Vicilin from cajanus cajan seeds

Phytochemistry, 1985
Abstract Vicilin from pigeon pea (Cajanus cajan) seeds was purified and characterised. It has a M, of ca 180 000 and consists of two types of subunits having M, s of ca 72 000 and 57 000. The subunits are not linked by disulphide bonds. The vicilin of pigeon pea differs from that of Pisum or Vicia in the absence of small M, subunits.
T.G. Krishna, C.R. Bhatia
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Antisickling Activity of Hydroxybenzoic Acids inCajanus cajan

Planta Medica, 1992
The amounts of phenylalanine and hydroxybenzoic acid in a Cajanus cajan methanolic extract were estimated. Results showed that the amount of phenylalanine and hydroxybenzoic acid per gram weight of bean was 4.92 mg +/- 0.13 mg and 21.0 mg +/- 3.0 micrograms, respectively.
F O, Akojie, L W, Fung
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Immobilization and stabilization of invertase on Cajanus cajan lectin support

Bioresource Technology, 2001
Use of lectins as ligands for the immobilization and stabilization of glycoenzymes has immense application in enzyme research and industry. But their widespread use could be limited by the high cost of their production. In the present study preparation of a novel and inexpensive lectin support for use in the immobilization of glycoenzymes containing ...
S, Ahmad, A, Anwar, M, Saleemuddin
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Prenylated stilbenes and flavonoids from the leaves of Cajanus cajan

Chinese Journal of Natural Medicines, 2019
Three new prenylated stilbenes, named as cajanusins A-C (1-3), and one new natural product cajanusin D (4), along with six known derivatives (5-10) were isolated from the leaves of Cajanus cajan. Their structures were fully elucidated by means of extensive spectroscopic methods and comparison with data in the reported literatures.
Gui-Yun, Wu   +8 more
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Characterization of a Proteinase Inhibitor from Cajanus cajan (L.)

Journal of Protein Chemistry, 2003
A protein proteinase inhibitor (PI) has been purified from pigeonpea Cajanus cajan (L.) PUSA 33 variety by acetic-acid precipitation, salt fractionation and chromatography on a DEAE-Cellulose column. The content of inhibitor was found to be 15 mg/20 g dry weight of pulse.
Soghra Khatun, Haq, Rizwan Hasan, Khan
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Unusual denaturation properties of vicilin from Cajanus cajan

Biochemical and Biophysical Research Communications, 1990
Pigeonpea (Cajanus cajan) vicilin (Mr 190 kD) holoprotein contains 2 subunits and the N-terminal amino acid sequence is Gly-Ala-Arg-Val-Asp-Gln-Glu for purified vicilin subunit 1 (Mr 72 kD) and Thr-Thr-Cys-Met-Glu-Ser-Gly for purified vicilin subunit 2 (Mr 57 kD).
Y R, Mawal, M R, Mawal, P K, Ranjekar
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