Solubilization and Partial Purification of Human Leukaemic Specific Antigens

Nature ◽  
1970 ◽  
Vol 227 (5264) ◽  
pp. 1249-1251 ◽  
Author(s):  
D. VIZA ◽  
D. A. L. DAVIES ◽  
R. HARRIS
Keyword(s):  
Partial Purification ◽  
Specific Antigens

Partial Purification of MS-Specific Antigens

1980 ◽  
pp. 221-231
Author(s):  
J. Clausen ◽  
S. C. Rastogi ◽  
H. Offner ◽  
G. Konat
Keyword(s):  
Partial Purification ◽  
Specific Antigens

Studies on liver specific antigens—partial purification, characterization, and immunization

1983 ◽  
Vol 18 (3) ◽  
pp. 232-240 ◽  
Author(s):  
Terukatsu Arima ◽  
Hiroyuki Shimomura ◽  
Hideo Nagashima
Keyword(s):  
Partial Purification ◽  
Liver Specific Antigens ◽  
Specific Antigens

Partial Purification of Multiple Sclerosis Specific Antigens

1979 ◽  
pp. 373-381
Author(s):  
S. C. Rastogi ◽  
J. Clausen ◽  
T. Fog ◽  
H. Offner ◽  
G. Konat
Keyword(s):  
Multiple Sclerosis ◽  
Partial Purification ◽  
Specific Antigens

Solubilization and partial purification of lymphocyte specific antigens in the chicken

1972 ◽  
Vol 2 (1) ◽  
pp. 30-35 ◽  
Author(s):  
D. Malchow ◽  
W. Droege ◽  
J. L. Strominger
Keyword(s):  
Partial Purification ◽  
Specific Antigens

Lectin Binding to Human Breast Tumor Cells

1976 ◽  
Vol 34 ◽  
pp. 34-35
Author(s):  
Robert E. Nordquist ◽  
J. Hill Anglin ◽  
Michael P. Lerner
Keyword(s):  
Carcinoma Cell ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Low Frequency ◽  
Breast Carcinoma Cell Line ◽  
Human Breast ◽  
Human Breast Tumor ◽  
Duct Carcinoma ◽  
Specific Antigens ◽  
Ricin Agglutinin

A human breast carcinoma cell line (BOT-2) was derived from an infiltrating duct carcinoma (1). These cells were shown to have antigens that selectively bound antibodies from breast cancer patient sera (2). Furthermore, these tumor specific antigens could be removed from the living cells by low frequency sonication and have been partially characterized (3). These proteins have been shown to be around 100,000 MW and contain approximately 6% hexose and hexosamines. However, only the hexosamines appear to be available for lectin binding. This study was designed to use Concanavalin A (Con A) and Ricinus Communis (Ricin) agglutinin for the topagraphical localization of D-mannopyranosyl or glucopyranosyl and D-galactopyranosyl or DN- acetyl glactopyranosyl configurations on BOT-2 cell surfaces.

Partial purification and properties of an endo-xylanase from cucumber seeds

1991 ◽  
Vol 81 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Cesar V. Mujer ◽  
Dale W. Kretchman ◽  
A. Raymond Miller
Keyword(s):  
Partial Purification ◽  
Purification And Properties

Partial purification and properties of a 36-kDa 1-aminocyclopropane-l-carboxylate N-malonyltransferase from mung bean

1995 ◽  
Vol 94 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Mohamed Benichou ◽  
Gracia Martinez-Reina ◽  
Felix Romojaro ◽  
Jean-Claude Pech ◽  
Alain Latche
Keyword(s):  
Mung Bean ◽  
Partial Purification ◽  
Purification And Properties

Characterization of HLA-A*0201 restricted cytotoxic CD8+ T cells directed against ewing tumor specific antigens

2009 ◽  
Vol 221 (03) ◽  
Author(s):  
S Pirson ◽  
U Thiel ◽  
H Bernhard ◽  
GHS Richter ◽  
S Burdach
Keyword(s):  
T Cells ◽  
Cd8 T Cells ◽  
Specific Antigens ◽  
Ewing Tumor

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Sign in / Sign up

Export Citation Format

Share Document