Abstract
Bovine serum lipoproteins were fractionated into high density and low and very low density lipoproteins by precipitation with sodium phosphotungstate and magnesium chloride. From each lipoprotein fraction seven apo C peptides were isolated by gel filtration and ion exchange chromatography. The two lipoprotein fractions probably contain identical apo C peptides but in different proportions. Two of the apo C peptides activated lipoprotein lipase from milk in vitro. Their specific activities were about 2000 times as high as that of the original serum. The apo C fraction from low-very low density lipoproteins had a specific activity three times that from high density lipoproteins. Also, the activator peptides from low and very low density lipoproteins gave one band on alkaline urea gel electrophoresis whereas corresponding peptides from high density lipoproteins were slightly heterogeneous. The low and very low density lipoproteins, therefore, seem to be the fraction of choice for isolation of activators for lipoprotein lipase.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
