Learn More
The fatty acid specificity of the bile salt-activated lipase purified from human milk was studied using C12 to C54 (total acyl carbon) saturated and the C54 unsaturated triacylglycerols. Kinetic studies indicated that the short chain triacylglycerols were hydrolyzed more readily than the long chain triacylglycerols, and that the long chain unsaturated(More)
The bone marrow stroma contains pre-adipocyte cells which are part of the hemopoietic microenvironment. Cloned stromal cell lines differ both in their ability to support myeloid and lymphoid development and in their ability to undergo adipocyte differentiation in vitro. These processes have been examined in the +/+2.4 murine stromal cell line and compared(More)
The bone marrow stroma consists of a heterogeneous population of cells which participate in osteogenic, adipogenic, and hematopoietic events. The murine stromal cell line, BMS2, exhibits the adipocytic and osteoblastic phenotypes in vitro. BMS2 differentiation was examined in response to cytokines which share the gp130 signal transducing protein within(More)
In this study we used monoacid triacylglycerols of various acyl-chain lengths as substrates for probing the active-site structure and substrate specificity of lipoprotein lipase (LPL). An unexpected finding was that the albumin ligand binding site is accessible not only to long-chain fatty acids for its recognized functional role as a fatty acid acceptor,(More)
Apolipoprotein E (ApoE; "arginine-rich" polypeptide) strongly inhibited both C-I and C-II activated lipoprotein lipases but not the protamine insensitive triglyceride lipase. Inhibition of lipoprotein lipases by ApoE in contrast to inhibition by C-III was not reversed to any significant extent by either increased concentration of activator or triglyceride(More)
In this study we have examined effects of synthetic polypeptide fragments of apoC-III on the kinetic properties of lipoprotein lipase (LPL) activity. Based on the loss of 79% of LPL-inhibitory activity after CNBr cleavage at the N-terminal portion of apoC-III and a systematic search for synthetic peptides with LPL-inhibitory activity spanning the apoC-III(More)
A modified heparin-Sepharose affinity chromatography procedure (Boberg et al., J. Lipid Res. 18:544-547, 1977) was developed to determine two different triglyceride lipase activities in human post-heparin plasma: hepatic triglyceride lipase (I) and lipoprotein lipase (II). With this procedure, lipoproteins were separated from the eluted lipases. The total(More)
Purified postheparin plasma lipoprotein lipase (LPL) of normolipidemic and primary hyperlipoproteinemic subjects was characterized by lipoprotein C polypeptide activation and specificity for triglycerides in chylomicrons and VLDL. Chromatography of normal LPL on Sephadex G-100 resulted in two protein peaks, LPLC-1 (activated by C-I but not C-II) and(More)
Purpose:A small supernumerary marker chromosome is often seen in patients with developmental disorders. Prior to array-based comparative genomic hybridization markers were rarely genotyped end to end. In this study, a valid genotype-to-phenotype correlation was possible because the supernumerary marker chromosomes were fully characterized by array-based(More)