TY - JOUR
T1 - Application of electron spin resonance to the study of the structure of human serum lipoproteins
AU - Gotto, Antonio
AU - Kon, H.
PY - 1969/10/22
Y1 - 1969/10/22
N2 - Human serum high density (HDL) and low density (LDL) lipoproteins were spin labeled with isothiocyanate and maleimide derivatives of the nitroxide radical N-(1-oxyl-2, 2, 6, 6-tetramethyl-4-piperidine). The ESR spectra of the HDL and LDL derivatives demonstrated at least two kinds of protein binding sites involving amino groups, one with slight and another with strong constraint on the tumbling of the nitroxide radical. There was relatively more of the strongly constrained component in labeled HDL than in LDL. The strongly immobilized signal was due to the binding of lipid as was shown by the effect of delipidation.
AB - Human serum high density (HDL) and low density (LDL) lipoproteins were spin labeled with isothiocyanate and maleimide derivatives of the nitroxide radical N-(1-oxyl-2, 2, 6, 6-tetramethyl-4-piperidine). The ESR spectra of the HDL and LDL derivatives demonstrated at least two kinds of protein binding sites involving amino groups, one with slight and another with strong constraint on the tumbling of the nitroxide radical. There was relatively more of the strongly constrained component in labeled HDL than in LDL. The strongly immobilized signal was due to the binding of lipid as was shown by the effect of delipidation.
UR - http://www.scopus.com/inward/record.url?scp=0014687946&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0014687946&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(69)90935-8
DO - 10.1016/0006-291X(69)90935-8
M3 - Article
C2 - 4310668
AN - SCOPUS:0014687946
SN - 0006-291X
VL - 37
SP - 444
EP - 450
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -