Molecular Biology of Human Proteins, with Special Reference to Plasma Proteins. Volume 1: Nature and Metabolism of Extracellular Proteins.H. E. Schultz , J. F. Heremans

1967 ◽  
Vol 42 (1) ◽  
pp. 80-81
Author(s):  
John T. Edsall
Keyword(s):  
Molecular Biology ◽  
Special Reference ◽  
Plasma Proteins ◽  
Human Proteins

Molecular Biology of the Acute Phase Plasma Proteins

Lymphokines ◽  
1987 ◽  
pp. 123-153 ◽  
Author(s):  
JONATHAN D. GITLIN ◽  
HARVEY R. COLTEN
Keyword(s):  
Molecular Biology ◽  
Acute Phase ◽  
Plasma Proteins

Endocytic Receptors in the Renal Proximal Tubule

Physiology ◽  
2012 ◽  
Vol 27 (4) ◽  
pp. 223-236 ◽  
Author(s):  
Erik I. Christensen ◽  
Henrik Birn ◽  
Tina Storm ◽  
Kathrin Weyer ◽  
Rikke Nielsen
Keyword(s):  
Molecular Biology ◽  
Proximal Tubule ◽  
Plasma Proteins ◽  
Animal Studies ◽  
Renal Proximal Tubule ◽  
Protein Clearance ◽  
Pathological Conditions ◽  
Protein Reabsorption

Protein reabsorption is a predominant feature of the renal proximal tubule. Animal studies show that the ability to rescue plasma proteins relies on the endocytic receptors megalin and cubilin. Recently, studies of patients with syndromes caused by dysfunctional receptors have supported the importance of these for protein clearance of human ultrafiltrate. This review focuses on the molecular biology and physiology of the receptors and their involvement in renal pathological conditions.

Bindings of plasma proteins to streptococci of serological group L with special reference to their immunoglobulin G Fc-receptor activity

1988 ◽  
Vol 34 (1) ◽  
pp. 1-5 ◽  
Author(s):  
C. Lämmler ◽  
P. Schaufuß ◽  
C. Frede ◽  
H. Blobel
Keyword(s):  
Affinity Chromatography ◽  
Special Reference ◽  
Molecular Mass ◽  
Immunoglobulin G ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fc Receptors ◽  
Streptococcus Dysgalactiae ◽  
Serological Group ◽  
Ig G

Of 33 streptococcal cultures belonging to serological group L, all bound human immunoglobulin (Ig) G, fibrinogen, and fibronectin; 32 bound bovine IgG; 31 bound α2-macroglobulin; 5 bound albumin; and none bound either haptoglobin or IgA. The binding sites for IgG could be isolated from the L streptococci by trypsinization and purified by affinity chromatography on human IgG – Sepharose®. The purified Fc receptors reacted with IgG subclasses 1, 2, 3, 4 of humans, 1 and 2 of bovines, ovines, and caprines as well as a, b, c, and T of equines. They had a molecular mass of approximately 49 000 Da. Thus, the Fc receptors from L streptococci corresponded to type III Fc receptors of Streptococcus dysgalactiae.

The choroid plexus in fetal sheep during development with special reference to intracellular plasma proteins

1983 ◽  
Vol 8 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Marianne Jacobsen ◽  
Kjeld Møllgård ◽  
Margaret L. Reynolds ◽  
Norman R. Saunders
Keyword(s):  
Special Reference ◽  
Choroid Plexus ◽  
Plasma Proteins ◽  
Fetal Sheep
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