Zobrazeno 1 - 10
of 88
pro vyhledávání: '"J S Parks"'
Autor:
K R Miller, J S Parks
Publikováno v:
Journal of Lipid Research, Vol 38, Iss 6, Pp 1094-1102 (1997)
Interfacial binding affinities and capacities of lecithin:cholesterol acyltransferase (LCAT) and apolipoprotein A-I (apoA-I) for surfaces of different phosphatidylcholine (PC) composition, cholesterol content, and apolipoprotein content were measured
Externí odkaz:
https://doaj.org/article/3a6cbc249c1544feaee5e4483df80644
Publikováno v:
Journal of Lipid Research, Vol 38, Iss 2, Pp 266-275 (1997)
The lecithin:cholesterol acyltransferase (LCAT) kinetics and activation energy and the stability of apolipoprotein A-I (apoA-I) were investigated using recombinant HDL (rHDL) containing phosphatidylcholine (PC), [3H]cholesterol, and apo A-I. The PC c
Externí odkaz:
https://doaj.org/article/b60ee78396e640c9a552b5c88a5e86ef
Autor:
R E Morton, J S Parks
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 9, Pp 1915-1923 (1996)
Previous studies have shown that lipid transfer protein (LTP) activity is strongly temperature dependent, demonstrating a dramatic rise in activity near 37 degrees C. We have investigated the origin of this rapid rise in LTP activity. LTP-mediated tr
Externí odkaz:
https://doaj.org/article/7c8868ca856f405c998a7f13725a7a87
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 3, Pp 551-561 (1996)
The glycosylation state of lecithin:cholesterol acyltransferase (LCAT) may be important in determining its enzymatic activity. We compared glycosylation structure, enzyme kinetics, and phosphatidylcholine (PC) acyl specificity of human LCAT from four
Externí odkaz:
https://doaj.org/article/0c39bda8b75846889a72388fe42b0075
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 3, Pp 673-683 (1996)
To facilitate the investigation of apoA-I structure:function relationships as they relate to LCAT activation and lipid binding, we have developed an apoA-I baculoviral expression and purification system that yields milligram quantities of wild-type o
Externí odkaz:
https://doaj.org/article/13ea2f0e049a46f394c5fa8379552781
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 6, Pp 1289-1297 (1996)
Recent studies using proton NMR to quantify plasma lipoprotein concentrations have shown that lipoprotein particle size affects the chemical shift of methyl and methylene resonances. The purpose of this study was to investigate the interrelationship
Externí odkaz:
https://doaj.org/article/a61aaf4f8a7446b387173b26ea5c40d5
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 2, Pp 277-289 (1995)
In the following report, cynomolgous monkeys, fed atherogenic diets containing either saturated, monounsaturated, polyunsaturated (n-6 Poly) or fish oil (n-3 Poly) fat as 35% of total calories, provide a model for the study of dietary fat effects on
Externí odkaz:
https://doaj.org/article/be5d04e815784be483e8509d51a856cd
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 2, Pp 349-355 (1995)
Plasma cholesteryl ester (CE) synthesis by lecithin cholesterol acyltransferase (LCAT) is activated by apolipoprotein (apo)A-I. We studied the effect of plasma apoA-I concentration on LCAT activation, using normal, heterozygous or homozygous apoA-I-d
Externí odkaz:
https://doaj.org/article/f44974168c2c453e9f970e34196cc182
Publikováno v:
Journal of Lipid Research, Vol 35, Iss 3, Pp 491-500 (1994)
In a previous study we demonstrated that isocaloric substitution of fish oil (FO) for lard in the diet of cynomolgus monkeys resulted in low density lipoproteins (LDL) that were poorer competitors for binding of a standard 125I-labeled LDL and led to
Externí odkaz:
https://doaj.org/article/d4dc8162ddcc447ca6312a48c977b8fe
Publikováno v:
Journal of Lipid Research, Vol 27, Iss 12, Pp 1304-1317 (1990)
The role of lecithin:cholesterol acyltransferase (LCAT) in the formation of plasma high density lipoproteins (HDL) was studied in a series of in vitro incubations in which perfusates from isolated African green monkey livers were incubated at 37 degr
Externí odkaz:
https://doaj.org/article/5ef44d6204684aa7bc597ed18e0afb07