73 research outputs found
Structural variations in actins. A study of the immunological reactivity of the N-terminal region
Structural variations in actins. Biochemical and immunological tools for probing the structure of rabbit skeletal-muscle and bovine aortic actins
cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells.
Actin antibodies. Preparation and characterization of antibodies specific for smooth-muscle actin isoforms
A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation
High-molecular-mass proteins in haemodialysis-associated amyloidosis
1. Protein constituents were determined in eight amyloid deposits from eight patients (five male and three female), 53 ± 4 years of age, treated by haemodialysis for 9-20 years using only cuprophane membranes and operated for carpal tunnel syndrome.
2. Soluble proteins were removed by solubilization in phosphate-buffered saline after osmotic lysis. The proteins of the insoluble fibrils were characterized by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and two-dimensional gel electrophoresis, and immunologically identified by Western blotting.
3. In addition to β2-microglobulin, α2-macroglobulin was identified in the fibrillar material. The presence of these two proteins in amyloid deposits was confirmed by immunofluorescent microscopic studies.
4. Our data confirm the presence of β2-microglobulin in haemodialysis-associated amyloidosis, and also suggest a possible role for α2-microglobulin: it may protect β2-microglobulin from proteolytic digestion, leading to its accumulation in intact form and to amyloid fibril formation.</jats:p
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