Vasoactivity of human plasma and plasma protein fractions

1968 ◽  
Vol 24 (11) ◽  
pp. 1126-1127 ◽  
Author(s):  
J. D. Horowitz ◽  
M. L. Mashford
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions

Heat Stable Human Plasma Protein Fractions Electrophoretically Rich in Albumin

Vox Sanguinis ◽  
1962 ◽  
Vol 7 (4) ◽  
pp. 406-413 ◽  
Author(s):  
E. H. Mealey ◽  
L. H. Larsen ◽  
R. C. Dwyer ◽  
D. J. Mulford
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions ◽  
Human Plasma Protein ◽  
Heat Stable

The Antigenic Nature of Heat-Treated Human Plasma Protein Fractions

Vox Sanguinis ◽  
1960 ◽  
Vol 5 (2) ◽  
pp. 122-137 ◽  
Author(s):  
John L. Lundblad ◽  
John H. Hink ◽  
Walter E. Ward ◽  
Ralph B. Houlihan ◽  
Paul L. Murphy
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions ◽  
Human Plasma Protein ◽  
Heat Treated

Generation of prothrombin-R with plasma protein fractions

1962 ◽  
Vol 202 (4) ◽  
pp. 664-670 ◽  
Author(s):  
Marion I. Barnhart ◽  
B. C. Das
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Specific Activity ◽  
Active Agent ◽  
Deae Cellulose ◽  
Protein Fractions ◽  
Beta Globulin ◽  
Plasma Fractions ◽  
Complete Regeneration ◽  
Prothrombin Activation

An activity of blood concerned in prothrombin activation is reported that was not previously recognized. Prothrombin-R was produced from a prothrombin derivative prepared with lysosomes after addition of various plasma fractions. The reaction was optimal at pH 7.9, and thrombin-C was not formed. Cohn fractions from either rabbit or human plasma generated prothrombin-R, although only fraction IV (alpha globulin plus) gave complete regeneration. Further purification of Cohn fractions was achieved with DEAE-cellulose chromatography. All fractions gave 100% yield of prothrombin-R. An immunoelectrophoretically pure alpha globulin had the highest specific activity. Partially purified gamma or beta globulin and albumin, also, were effective in that order. Immunologic data support the view that the alpha globulin content of these other fractions was responsible for generation of prothrombin-R. Most likely the active agent is an enzyme. Accordingly the plasma constituent which generates prothrombin-R is designated enzyme-R.

Heat Stable Human Plasma Protein Fractions Electrophoretically Rich in Albumin

Vox Sanguinis ◽  
1962 ◽  
Vol 7 (4) ◽  
pp. 406-413
Author(s):  
E.H. Mealey ◽  
L.H. Larsen ◽  
R.C. Dwyer ◽  
D.J. Mulford
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions ◽  
Human Plasma Protein ◽  
Heat Stable

Inhibition of platelet [3H]-imipramine binding by human plasma protein fractions

Life Sciences ◽  
1988 ◽  
Vol 42 (16) ◽  
pp. 1543-1550 ◽  
Author(s):  
Achim Strijewski ◽  
Jerzy Chudzik ◽  
Siu Wa Tang
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions ◽  
Human Plasma Protein ◽  
Imipramine Binding

The Antigenic Nature of Heat-Treated Human Plasma Protein Fractions

Vox Sanguinis ◽  
1960 ◽  
Vol 5 (2) ◽  
pp. 122-137
Author(s):  
John L. Lundblad ◽  
John Hink ◽  
Walter E. Ward ◽  
Ralph B. Houlihan ◽  
Paul L. Murphy
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Protein Fractions ◽  
Human Plasma Protein ◽  
Heat Treated

scholarly journals A western blot approach to detection of human plasma protein conjugates derived from D-penicillamine.

1994 ◽  
Vol 53 (4) ◽  
pp. 256-260 ◽  
Author(s):  
C A Laycock ◽  
M J Phelan ◽  
R C Bucknall ◽  
J W Coleman
Keyword(s):  
Western Blot ◽  
Human Plasma ◽  
Plasma Protein ◽  
Protein Conjugates ◽  
Human Plasma Protein
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