Related Articles1H NMR-based absolute quantitation of human lipoproteins and their lipid contents directly from plasma.
J Lipid Res. 1994 Dec;35(12):2292-304
Authors: Ala-Korpela M, Korhonen A, Keisala J, Hörkkö S, Korpi P, Ingman LP, Jokisaari J, Savolainen MJ, Kesäniemi YA
A new method is presented for absolute quantitation of lipid and protein contents of human lipoproteins directly from plasma. The method enables complete lipoprotein lipid profiles to be obtained in a total time of less than one hour. Absolute concentrations of triglycerides, phospholipids, total cholesterol, free cholesterol, esterified cholesterol, total proteins, and total masses can be estimated for the very low density (VLDL) and low density (LDL) lipoprotein fractions. For the high density lipoprotein (HDL) fraction all components except triglycerides can be quantitated. The method is a combination of 1H NMR spectroscopy and a sophisticated lineshape fitting analysis technique. In this paper we present the calibration of the method using 15 plasma samples followed by a double-blind test of 51 plasma samples from 43 individuals. In total, 66 plasma samples were analyzed. Comparison of the 1H NMR-based results with the data of the biochemical assays showed excellent agreement; the correlation coefficient for VLDL triglycerides was 0.98, for LDL cholesterol 0.88, and for HDL cholesterol 0.93. This method can be directly integrated to many kinds of biomedical NMR studies to offer additional biochemically important quantitative lipoprotein information, the measurement of which is usually too laborious by conventional biochemical methods and too high-priced to be adapted into the study protocols. Moreover, the method also has considerable potential to be developed for a routine clinical assay.
[NMR paper] GFT NMR based resonance assignment for the 21 kDa human protein UFC1.
GFT NMR based resonance assignment for the 21 kDa human protein UFC1.
Related Articles GFT NMR based resonance assignment for the 21 kDa human protein UFC1.
J Biomol NMR. 2005 Jul;32(3):261
Authors: Liu G, Aramini J, Atreya HS, Eletsky A, Xiao R, Acton T, Ma L, Montelione GT, Szyperski T
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[NMR paper] Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
Related Articles Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
J Lipid Res. 2001 Sep;42(9):1501-8
Authors: Schiller J, Zschörnig O, Petkovi? M, Müller M, Arnhold J, Arnold K
The analysis of HDL and LDL is important for the further understanding of atherosclerosis because changes of the protein and lipid moieties occur under pathological conditions. Because destruction of lipids leads to the formation of well-defined products...
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Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR
Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Related Articles Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Chem Phys Lipids. 2010 Jun;163(6):545-51
Authors: Gómez SL, Monteiro AM, Rabbani SR, Bloise AC, Carneiro SM, Alves S, Gidlund M, Abdalla DS, Neto AM
In this work we report on a study of the morphological changes of LDL induced in vitro by metallic ions (Cu(2+) and Fe(3+)). These modifications were...
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[NMR paper] NMR-based discovery of lead inhibitors that block DNA binding of the human papillomav
NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein.
J Med Chem. 1997 Sep 26;40(20):3144-50
Authors: Hajduk PJ, Dinges J, Miknis GF, Merlock M, Middleton T, Kempf DJ, Egan DA, Walter KA, Robins TS, Shuker SB, Holzman TF, Fesik SW
The E2 protein is required for the replication of human...
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[NMR paper] A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of s
A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
Biochemistry. 1996 Apr 9;35(14):4540-50
Authors: Modi S, Paine MJ, Sutcliffe MJ, Lian LY, Primrose WU, Wolf CR, Roberts GC
The cytochrome P450 responsible for the debrisoquine/sparteine polymorphism (P450 2D6) has been produced in large...
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[NMR paper] 1H NMR-based determination of the three-dimensional structure of the human plasma fib
1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
Related Articles 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
J Biol Chem. 1993 Apr 25;268(12):8580-9
Authors: Kar L, Lai CS, Wolff CE, Nettesheim D, Sherman S, Johnson ME
Human plasma fibronectin is a plasma glycoprotein that plays an important role in many biological processes. It consists of two...
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[NMR paper] Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid
Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Related Articles Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Biochemistry. 1990 Apr 24;29(16):3828-34
Authors: Van Gorkom LC, Horváth LI, Hemminga MA, Sternberg B, Watts A
The major coat protein of M13 bacteriophage has been incorporated into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine, deuterated in the trimethyl segments of...
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[NMR paper] Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the
Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Related Articles Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Biochem Cell Biol. 1990 Jan;68(1):189-98
Authors: Chana RS, Treleaven WD, Parmar YI, Cushley RJ
The order of phosphatidylcholine (PC) acyl chains in the surface monolayer of very low density lipoproteins (VLDL) and low density lipoproteins (LDL) has been...