Isolation and characterization of β-galactoside specific lectin from Korean mistletoe (Viscum album var.coloratum) with lactose-BSA-Sepharose 4B and changes of lectin conformation

1998 ◽  
Vol 21 (4) ◽  
pp. 429-435 ◽  
Author(s):  
Won Bong Park ◽  
Yeun Jin Ju ◽  
Seon Kyu Han
Keyword(s):  
Viscum Album ◽  
Korean Mistletoe ◽  
Isolation And Characterization ◽  
Sepharose 4B

scholarly journals Studies on gastric mucoproteins. The isolation and characterization of the mucoprotein of the water-soluble mucus from pig cardiac gastric mucosa

1971 ◽  
Vol 123 (5) ◽  
pp. 845-853 ◽  
Author(s):  
D. Snary ◽  
A. Allen
Keyword(s):  
Sialic Acid ◽  
Gastric Mucosa ◽  
Gel Filtration ◽  
Water Soluble ◽  
Group Activities ◽  
Isolation And Characterization ◽  
Two Peaks ◽  
Sepharose 4B

1. Gel filtration of the water-soluble radioactive mucus produced three radioactive fractions, fraction A excluded on Sepharose 4B, fraction B included on Sepharose 4B but excluded on Sephadex G-200, and fraction C included on Sephadex G-200. 2. The specific radioactivities of fractions A and B were the same, with fraction C a little lower, whether the material was labelled with 14C-labelled carbohydrate or with 3H-labelled protein prepared by incubation of mucosal scrapings in vitro with [U-14C]glucose or [G-3H]threonine respectively. 3. Fractions A and B had an analysis of protein 22%, hexose 28%, hexosamine 28%, fucose 10% and sialic acid 1%; fraction C had an analysis closely similar to this, except that it contained about 10% of a protein contaminant. 4. All three fractions had closely similar A and H blood-group activities. 5. Ultracentrifuge studies showed fractions A, B and C were polydisperse with s025,w values of 18.7S, 4.9S and 3.9S respectively. 6. The unfractionated water-soluble mucus contained only two peaks, fraction A 18.7S and a peak of 4.4S, which was a combination of fractions B and C. 7. The radioactive mucoprotein accounted for 85% by weight of the soluble mucus and the results show that it consisted of two distinct fractions A and B–C, which were chemically, biosynthetically and immunologically very similar.

scholarly journals Isolation and characterization of viscumin, a toxic lectin from Viscum album L. (mistletoe).

1982 ◽  
Vol 257 (22) ◽  
pp. 13263-13270 ◽  
Author(s):  
S Olsnes ◽  
F Stirpe ◽  
K Sandvig ◽  
A Pihl
Keyword(s):  
Viscum Album ◽  
Isolation And Characterization

scholarly journals Isolation and Characterization of Two Korean Mistletoe Lectins

BMB Reports ◽  
2007 ◽  
Vol 40 (6) ◽  
pp. 959-965 ◽  
Author(s):  
Tae-Bong Kang ◽  
Seong-Kyu Song ◽  
Taek-Joon Yoon ◽  
Yung-Choon Yoo ◽  
Kwan-Hee Lee ◽  
...  
Keyword(s):  
Korean Mistletoe ◽  
Isolation And Characterization

scholarly journals Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin

1983 ◽  
Vol 211 (3) ◽  
pp. 661-670 ◽  
Author(s):  
M Brett ◽  
J B C Findlay
Keyword(s):  
Staphylococcus Aureus ◽  
Gel Permeation Chromatography ◽  
Isolation And Characterization ◽  
Peptide Mixture ◽  
Gel Permeation ◽  
Membrane Bound ◽  
Sepharose 4B ◽  
Differential Solubility

Ovine rhodopsin may be cleaved in situ by Staphylococcus aureus V8 proteinase into two membrane-bound fragments designated V8-L (27 000 mol.wt.) and V8-S (12 000 mol.wt.). After purification of the proteolysed complex by affinity chromatography in detergent using concanavalin A immobilized on Sepharose 4B, the two polypeptide fragments may be separated by gel-permeation chromatography on Sephadex LH-60. Digestion of the N-terminal-derived V8-L fragment with CNBr in 70% (v/v) trifluoroacetic acid resulted in a peptide mixture that could be fractionated by procedures involving gel-permeation chromatography in organic and aqueous solvents and the use of differential solubility. The complete or partial sequences of all ten peptides are reported.

scholarly journals Isolation and characterization of sheep pepsin

1977 ◽  
Vol 161 (2) ◽  
pp. 389-398 ◽  
Author(s):  
P F Fox ◽  
J R Whitaker
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Ethyl Ester ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Sepharose 4B ◽  
Hydrolysis Of

Sheep pepsin was isolated (approx. 120-fold purification) from aqueous abomasal homogenates by (1) pH fractionation, (2) chromatography on Sepharose 4B-poly-L-lysine columns and (3) gel filtration on Sephadex G-100. The enzyme had mol.wt. approx. 34000, N-terminal valine and C-terminal alanine. The amino acid composition of sheep pepsin was generally similar to that of pig and ox pepsins, with a very low content of basic residues and a high content of acidic and hydroxy-amino acids. The pH optimum for NN-dimethyl-casein and NN-dimethyl-haemoglobin as substrates was approx. 1.8. The Km and kcat. for NN-dimethyl-haemoglobin were 46micronM and 1100min-1 respectively, and for NN-dimethyl-casein the corresponding parameters were 50micronM and 420min-1. These values were generally similar to those for pig and ox pepsins. At the pH optimum of 4.6, the sheep pepsin was about 50% as active on benzyloxycarbonyl-L-histidyl-L-phenyl-alanyl-L-tryptophan ethyl ester as was pig pepsin. The pH optimum for the hydrolysis of N-acetyl-L-phenylalanyl-L-di-iodotyrosine by sheep, ox and pig pepsins was approx. 1.85.

The isolation and characterization of 18 equine microsatellite loci, TKY272–TKY289

2000 ◽  
Vol 31 (2) ◽  
pp. 149-149 ◽  
Author(s):  
T Tozaki ◽  
H Kakoi ◽  
S Mashima ◽  
K Hirota ◽  
T Hasegawa ◽  
...  
Keyword(s):  
Microsatellite Loci ◽  
Isolation And Characterization
Sign in / Sign up

Export Citation Format

Share Document