Wheat germ lectin induces G2/M arrest in mouse L929 fibroblasts

2004 ◽  
Vol 91 (6) ◽  
pp. 1159-1173 ◽  
Author(s):  
W.K. Liu ◽  
S.C.W. Sze ◽  
J.C.K. Ho ◽  
B.P.L. Liu ◽  
M.C. Yu
Keyword(s):  
Wheat Germ ◽  
Wheat Germ Lectin

scholarly journals Aggregation of casein micelle from bovine milk by wheat germ lectin.

1978 ◽  
Vol 42 (10) ◽  
pp. 1923-1926 ◽  
Author(s):  
Masaaki YOSHIKAWA ◽  
Kyoya TAKAHATA ◽  
Ryuzo SASAKI ◽  
Hideo CHIBA
Keyword(s):  
Wheat Germ ◽  
Bovine Milk ◽  
Casein Micelle ◽  
Wheat Germ Lectin

Lectins as Cytochemical Probes of the Developing Wheat Grain. V. Demonstration of Separate Polysaccharides Containing N-Acetyl-D-Glucosamine and D-Galactose in Nuclear Epidermal Cell Walls

1984 ◽  
Vol 11 (3) ◽  
pp. 179 ◽  
Author(s):  
BA Baldo ◽  
D Barnett ◽  
JW Lee
Keyword(s):  
Epidermal Cell ◽  
Cell Walls ◽  
Wheat Germ ◽  
Periodic Acid ◽  
Fluorescein Isothiocyanate ◽  
Wheat Grain ◽  
Periodic Acid Schiff ◽  
Thin Sections ◽  
Lectin Staining ◽  
Wheat Germ Lectin

Fluorescein isothiocyanate-labelled lectin from wheat-gem, which binds N-acetyl-D-glucosamine, and Griffonia simplicifolia, Arachis hypogaea and Glycine max lectins, each of which binds D-galactose, react with nucellar epidermal cell walls in thin sections of plastic-embedded developing wheat grain. Reactivity of these cell walls with periodic acid-Schiff reagent, the absence of staining with protein stains and the failure of a number of proteases and the endoglycosidases D and H to prevent the binding suggested that the lectin-reactive wall components are neither proteins nor N-glycosidically linked glycoproteins. Morphological differences in lectin staining patterns and treatment of sections with chitinase and α-galactosidase, prior to the reaction with the lectins, indicated that two separate polysaccharides are probably involved in the binding. Chitinase removed the reactivity of the nucellar epidermal cell walls for wheat-germ lectin but the binding of D-galactose-specific lectins was unimpaired. Conversely, α-galactosidase did not affect the binding of wheat-germ lectin but reactivity with the galactose-specific lectins was abolished. From the available evidence we conclude that one polysaccharide in the nucellar epidermal cell wall reacts with wheat-germ lectin and contains N-acetyl-D-glucosamine in a chitin-like structure. The other polysaccharide reacts with D-galactose- specific lectins by virtue of terminal α-D-galactose residues. Hydrolysis and subsequent chromatographic analysis of nucellar epidermal cell walls peeled from immature grains revealed the presence of D-glucosamine, D-glucose, D-galactose, D-xylose, L-arabinose and a trace of D-mannose.

Wheat germ lectin affinity electrophoresis of serum alkaline phosphatase with commercially available agarose gels

1993 ◽  
Vol 39 (7) ◽  
pp. 1404-1407 ◽  
Author(s):  
M Mattiazzo ◽  
I Ramasamy
Keyword(s):  
Alkaline Phosphatase ◽  
Wheat Germ ◽  
Serum Alkaline Phosphatase ◽  
Single Step ◽  
Agarose Gels ◽  
Lectin Affinity ◽  
Affinity Electrophoresis ◽  
Alkaline Phosphatase Isoenzymes ◽  
Electrophoresis Method ◽  
Wheat Germ Lectin

Abstract We have modified a commercially available procedure involving precast agarose gels (Paragon Isopal System) to measure alkaline phosphatase (EC 3.1.3.1) isoenzymes. Including wheat germ lectin in the equilibration buffer improved the resolution of the bone and liver isoenzymes. Unlike previously described wheat germ lectin affinity electrophoresis methods, the procedure measures bone, liver, and biliary isoenzymes in a single step. There was good correlation between the affinity electrophoresis and the neuraminidase preincubation methods for the measurement of bone (r = 0.958) and liver (r = 0.962) alkaline phosphatase isoenzymes. However, the affinity electrophoresis method also quantified minor isoenzyme fractions that were poorly resolved by the neuraminidase method. The method is technically simple, reproducible, and capable of rapid handling of large workloads.

Quantification of bone alkaline phosphatase in serum by precipitation with wheat-germ lectin: a simplified method and its clinical plausibility.

1986 ◽  
Vol 32 (10) ◽  
pp. 1960-1966 ◽  
Author(s):  
W Behr ◽  
J Barnert
Keyword(s):  
Alkaline Phosphatase ◽  
Wheat Germ ◽  
Biliary Tree ◽  
Bone Alkaline Phosphatase ◽  
Original Method ◽  
Bone Diseases ◽  
Skeletal Involvement ◽  
Number Of Patients ◽  
Comparison Groups ◽  
Wheat Germ Lectin

Abstract We report an easy, rapid method for quantifying bone isoenzyme of alkaline phosphatase (EC 3.1.3.1., ALP) in serum. The original method described by Rosalki and Ying Foo (Clin Chem 1984;30:1182-6) was somewhat simplified. In contrast to their results, we found that bone ALP is precipitated quantitatively by wheat-germ lectin. To check the clinical plausibility of the method, we used samples from several comparison groups (blood donors, children, pregnant women, patients with neoplasms but without skeletal involvement) and a large number of patients suffering from bone diseases and diseases of the liver and biliary tree. Measured activities of bone ALP nearly always correlated with the clinical diagnosis. Only patients with hepatitis often had pathological bone activities not in accord with the other findings. Possible reasons for this observation are discussed.

Precipitation of serum proteins by the lectin from wheat-germ.

1987 ◽  
Vol 33 (1) ◽  
pp. 185-186 ◽  
Author(s):  
W E Schreiber ◽  
L Whitta
Keyword(s):  
Alkaline Phosphatase ◽  
Serum Protein ◽  
Wheat Germ ◽  
Serum Proteins ◽  
Total Serum Protein ◽  
Total Serum ◽  
Wheat Germ Lectin

Abstract We investigated the composition of the precipitate that forms when wheat-germ lectin derived from Triticum vulgaris is added to serum. A number of serum proteins are precipitated, representing about 2.5% of the total serum protein. This study demonstrates that the interaction of this lectin with the bone isoenzyme of alkaline phosphatase is not specific.

scholarly journals Immunogenetics of a macroglobulin allotype in cattle

1978 ◽  
Vol 31 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Domenico Iannelli ◽  
Piero Masina
Keyword(s):  
Isoelectric Point ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Serum Antigen ◽  
Cattle Serum ◽  
The One ◽  
Wheat Germ Lectin

SUMMARYThe paper describes a cattle serum antigen (McA2) located on a macroglobulin molecule which has its isoelectric point at pH 5 and is capable of interacting with the wheat germ lectin and concanavalin A.The specificity is inherited in a simple Mendelian manner and the gene controlling its synthesis is allelic to the one controlling the synthesis of the McAl antigen.

Sign in / Sign up

Export Citation Format

Share Document