Similar Effects of Toluene and Dibucaine on Human Platelet Membrane Glycoprotein Ib and Actin-Binding Protein

1991 ◽  
Vol 625 (1 Molecular and) ◽  
pp. 835-836
Author(s):  
ANNE SMITH-KIELLAND ◽  
ANNE MARGRETHE AAKHUS ◽  
ÅSE RIPEL ◽  
NILS O. SOLUM
Keyword(s):  
Human Platelet ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Actin Binding ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Actin Binding Protein ◽  
Platelet Membrane Glycoprotein

Effects of toluene on platelet membrane glycoprotein Ib and actin-binding protein

1991 ◽  
Vol 42 (4) ◽  
pp. 805-811 ◽  
Author(s):  
Anne M. Aakhus ◽  
Anne Smith-Kielland ◽  
Aase Ripel ◽  
Nils Olav Solum
Keyword(s):  
Binding Protein ◽  
Platelet Membrane ◽  
Actin Binding ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Actin Binding Protein ◽  
Platelet Membrane Glycoprotein

Cleavage site of calcium-dependent protease in human platelet membrane glycoprotein ib

1986 ◽  
Vol 43 (1) ◽  
pp. 41-55 ◽  
Author(s):  
Kazuo Yamamoto ◽  
Goro Kosaki ◽  
Koichi Suzuki ◽  
Kenjiro Tanoue ◽  
Hiroh Yamazaki
Keyword(s):  
Cleavage Site ◽  
Human Platelet ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Calcium Dependent ◽  
Platelet Membrane Glycoprotein

Glycoprotein Ib- and actin-binding regions in human platelet actin-binding protein

1991 ◽  
Vol 19 (4) ◽  
pp. 1133-1134 ◽  
Author(s):  
Anne M. Aakhus ◽  
J. Michael Wilkinson ◽  
Nils O. Solum
Keyword(s):  
Human Platelet ◽  
Binding Protein ◽  
Actin Binding ◽  
Glycoprotein Ib ◽  
Actin Binding Protein ◽  
Binding Regions

Localization of a Thrombin-Binding Site on Human Platelet Membrane Glycoprotein Ib Determined by a Monoclonal Antibody

1986 ◽  
Vol 55 (02) ◽  
pp. 162-167 ◽  
Author(s):  
K Yamamoto ◽  
N Yamamoto ◽  
H Kitagawa ◽  
K Tanoue ◽  
G Kosaki ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Affinity Chromatography ◽  
Binding Site ◽  
Cleavage Site ◽  
Human Platelet ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Platelet Membrane Glycoprotein

SummaryTo determine a thrombin-binding site on GPIbα on platelet membrane, we have examined the binding activities of tryptic or chymotryptic fragments of purified GPIbα to a monoclonal antibody against GPIb (TM60) and thrombin using (immuno) affinity chromatography. When purified GPIba was digested with trypsin, two fragments (94-kDa, and 43-kDa) were obtained. The 43-kDa fragment was shown to bind to both affinity columns of TM60- and thrombin-Affi-Gel, while the 94-kDa fragment did not bind to either Affi-Gel columns. When trypsin fragments were incubated with TM60 and then applied to the column of thrombin-Affi-Gel, neither fragments were bound to the column. When the same experiment was performed using chymotrypsin, three fragments (94-kDa, 45-kDa and 39-kDa) were observed. On TM60- and thrombin-Affi-Gel columns, the smaller fragments (45-kDa and 39-kDa) were bound to the column. After incubation of these fragments with TM60, neither bound to the thrombin column. These results indicate (i) that the epitope for TM60 is located near, or on the thrombin-binding site of GPIba, and (ii) that the thrombin-binding site is located on the tail portion of GPIbα, especially on a chymotrypsin cleavage site.

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