Proteins of human urine. III. Identification and two-dimensional electrophoretic map positions of some major urinary proteins
The proteins of human urine have been mapped by high-resolution two-dimensional electrophoresis, utilizing the ISO-DALT system. Wide-range pH gradients and narrow-range acid gradients were both used in the first-dimension separations. The patterns revealed proteins ranging in relative molecular mass from 10 000 to 90 000. Proteins identified in the map included transferrin, albumin, hemopexin, ..cap alpha../sub 2/-HS glycoprotein, ..cap alpha../sub 1/-antitrypsin, Gc globulin, ..cap alpha../sub 1/-acid glycoprotein, Zn ..cap alpha../sub 2/-glycoprotein, retinol binding protein, ..beta../sub 2/-microglobulin, the immunoglobulin light chains, and MAUP (most acid urinary protein). The use and utility of internal-charge and molecular-mass standards are described. We used electrophoretic transfer of proteins to nitrocellulose sheets and subsequent detection by immunological methods to identify some proteins.
- Research Organization:
- Argonne National Lab., IL
- DOE Contract Number:
- W-31-109-ENG-38
- OSTI ID:
- 5032360
- Journal Information:
- Clin. Chem. (Winston-Salem, N.C.); (United States), Vol. 28:4
- Country of Publication:
- United States
- Language:
- English
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ELECTROPHORESIS
DIAGNOSTIC USES
PROTEINS
URINE
ALBUMINS
GLUCOPROTEINS
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MAN
MOLECULAR WEIGHT
NITROCELLULOSE
PH VALUE
TRANSFERRIN
ANIMALS
BIOLOGICAL MATERIALS
BIOLOGICAL WASTES
BODY FLUIDS
CARBOHYDRATES
CELLULOSE ESTERS
CHEMICAL EXPLOSIVES
ESTERS
EXPLOSIVES
GLOBULINS
GLOBULINS-BETA
MAMMALS
MATERIALS
METALLOPROTEINS
NITRIC ACID ESTERS
ORGANIC COMPOUNDS
POLYSACCHARIDES
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VERTEBRATES
WASTES
550200* - Biochemistry