scholarly journals Heparin-inhibitable lectin. Purification from chicken liver and embryonic chicken muscle.

1981 ◽  
Vol 256 (1) ◽  
pp. 390-394
Author(s):  
H. Ceri ◽  
D. Kobiler ◽  
S.H. Barondes
Keyword(s):  
Chicken Liver ◽  
Embryonic Chicken ◽  
Chicken Muscle ◽  
Lectin Purification

The Comparative Enzymology of Lactic Dehydrogenases. II. Properties of the Crystalline HM3Hybrid from Chicken Muscle and of H2M2Hybrid and H4Enzyme from Chicken Liver*

Biochemistry ◽  
1964 ◽  
Vol 3 (4) ◽  
pp. 522-530 ◽  
Author(s):  
Thomas P. Fondy ◽  
Amadeo Pesce ◽  
Irwin Freedberg ◽  
Francis Stolzenbach ◽  
Nathan O. Kaplan
Keyword(s):  
Chicken Liver ◽  
Chicken Muscle ◽  
Comparative Enzymology

Non-histone chromatin protein fractions associated with ‘active’ chromatin in embryonic chicken liver

1985 ◽  
Vol 65 (2) ◽  
pp. 131-141
Author(s):  
Barbara Siemieniako ◽  
Ewa M. Rakowicz-Szulczyńska ◽  
Antoni Horst
Keyword(s):  
Protein Fractions ◽  
Chicken Liver ◽  
Chromatin Protein ◽  
Active Chromatin ◽  
Embryonic Chicken

scholarly journals Determination of Chloramphenicol Residue in Chicken Tissues by Immunoaffinity Chromatography Cleanup and Gas Chromatography with aMicrocell Electron Capture Detector

2006 ◽  
Vol 89 (2) ◽  
pp. 369-373 ◽  
Author(s):  
Suxia Zhang ◽  
Jinhui Zhou ◽  
Jianzhong Shen ◽  
Shuangyang Ding ◽  
Jiancheng Li
Keyword(s):  
Gas Chromatography ◽  
Electron Capture ◽  
Chicken Liver ◽  
Electron Capture Detector ◽  
Immunoaffinity Column ◽  
Chicken Tissues ◽  
Chicken Muscle ◽  
Limit Of Quantitation ◽  
Sepharose 4B

Abstract A rapid and sensitive gas chromatography (GC) method was developed to detect chloramphenicol in chicken tissues. The extracted samples were cleaned up using the immunoaffinity column prepared by coupling antichloramphenicol monoclonal antibody with cyanogen bromide-activated Sepharose 4B. The dynamic column capacity of chloramphenicol was 3265 ng/mL gel. The eluate was evaporated to dryness, and residues were derivatized and determined by GC with a microcell electron capture detector. Average recoveries were 86.6 to 96.9 for chicken muscle and 74.3 to 96.1 for chicken liver. The limit of quantitation of the method was 0.05 ng/g for chicken muscle and 0.1 ng/g for chicken liver.

scholarly journals Comparative rates of transfer of N-acetylneuraminic acid to acceptors bearing one or more Gal(β 1-4)GlcNAc terminus by the Gal(β 1-4)GlcNAc(NeuAc-Gal) (α 2-6)-sialyltransferase from embryonic chicken liver. Utilization of oligosaccharides as acceptors in sialyltransferase assays

1983 ◽  
Vol 213 (1) ◽  
pp. 253-260 ◽  
Author(s):  
B Bendiak ◽  
G M W Cook
Keyword(s):  
Relative Orientation ◽  
Chicken Liver ◽  
Acid Glycoprotein ◽  
Acetylneuraminic Acid ◽  
Embryonic Chicken ◽  
Acid Protein ◽  
Marked Preference ◽  
Km Value ◽  
Glcnac Termini

Using a number of branched and unbranched oligosaccharides, glycoproteins and artificial glycoproteins bearing Gal(beta 1-4)GlcNAc-R termini as acceptors (where R represents H, oligosaccharide, oligosaccharide-protein or fatty acid-protein), the comparative rates of transfer of NeuAc by the Gal(beta 1-4)GlcNAc(NeuAc-Gal) (alpha 2-6)-sialyltransferase of embryonic chicken liver were determined. Acceptor substrates were utilized at levels approximating physiological, near the Km value of the best acceptor, desialylated alpha 1 acid glycoprotein. The sialyltransferase has a marked preference for multi-branched acceptors. From the specificity data, it is concluded that the enzyme binds at least two Gal(beta 1-4)GlcNAc termini of an acceptor molecule, and that the relative orientation of the branches is an important factor determining the rate of catalysis by the enzyme. The use of oligosaccharides as acceptors to study sialyltransferase catalyses is emphasized. Results are discussed in the context of the mode of assembly of sialoside termini of known glycoprotein structures in vivo.

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