منابع مشابه
Electrophoretic studies on human serum.
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متن کاملOn the structure of human serum high-density lipoprotein: studies by the technique of circular dichroism.
Previous studies from this laboratory employing the technique of optical rotatory dispersion (ORD) have shown that human serum high-density lipoprotein (HDL) of d 1.063-1.21 gm/ml has a high content in a-helix which is to a large extent retained in its lipid-free form, apo HDL.1 On the basis of the ORD parameters, an unordered structure was assigned to the nonhelical portion of the apoprotein, ...
متن کاملActivation of lipoprotein lipase by lipoprotein fractions of human serum.
Triglycerides in fat emulsions are hydrolyzed by lipoprotein lipase only when they are "activated" by serum lipoproteins. The contribution of different lipoprotein fractions to hydrolysis of triglycerides in soybean oil emulsion was assessed by determining the quantity of lipoprotein fraction required to give half-maximal hydrolysis. Most of the activator property of whole serum from normolipid...
متن کاملStudies on human serum paraoxonase/arylesterase.
The complete amino acid sequence of human serum paraoxonase/arylesterase and the DNA sequence coding for that protein have recently been determined in two independent laboratories. There is now considerable evidence that the esterase exists in two genetically determined allozymic forms, and these A and B allozymes possess both paraoxonase and arylesterase activities. The B-type esterase has rel...
متن کاملStudies on Human Serum High Density Lipoproteins
Human serum apolipoprotein A-I (ape-A-I), the major protein component of the human serum high density lipoproteins, was studied in aqueous solutions of differing ionic strengths and pH by the techniques of sedimentation equilibrium ultracentrifugation and frontal analysis gel chromatography. The ultracentrifugal studies indicate that apo-A-I is a self-associating system that is dependent upon p...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96943-7