TY - JOUR
T1 - The cyanogen bromide peptides of the apoprotein of low density lipoprotein (apoB)
T2 - Its molecular weight from a chemical view
AU - Bradley, W. A.
AU - Rohde, M. F.
AU - Gotto, Antonio
AU - Jackson, R. L.
N1 - Funding Information:
This research was supported by the Atherosclerosis, Lipids and Lipoproteins section of the National Heart and Blood Vessel Research and Demonstration Center, Baylor College of Medicine, a grant-supported research project of the National Heart, Lung, and Blood Institute, National Institutes of Health, Grant No. HL 17269. We acknowledge the assistance of Ms. Debbie Mason in preparing the manuscript and Ms. Kaye Shewmaker in preparing the figures.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1978/4/14
Y1 - 1978/4/14
N2 - After >95% cleavage of the apoprotein (apoB) of the low density lipoproteins with cyanogen bromide, the peptides produced are shown to be extensively aggregated in sodium dodecyl sulfate. Both high temperature and increased concentration (5%) of the detergent are necessary to shift the aggregated peptides from high molecular weight (>25,000) to lower molecular weight aggregates as seen on sodium dodecyl sulfate polyacrylamide gel electrophoresis. End group analyses of the cyanogen bromide digestion by automated sequencer techniques indicate the presence of five (5) methionines. With a known methionine content of 16 moles/100,000 g protein, the molecular weight of the apoprotein must be approximately 30,000.
AB - After >95% cleavage of the apoprotein (apoB) of the low density lipoproteins with cyanogen bromide, the peptides produced are shown to be extensively aggregated in sodium dodecyl sulfate. Both high temperature and increased concentration (5%) of the detergent are necessary to shift the aggregated peptides from high molecular weight (>25,000) to lower molecular weight aggregates as seen on sodium dodecyl sulfate polyacrylamide gel electrophoresis. End group analyses of the cyanogen bromide digestion by automated sequencer techniques indicate the presence of five (5) methionines. With a known methionine content of 16 moles/100,000 g protein, the molecular weight of the apoprotein must be approximately 30,000.
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U2 - 10.1016/0006-291X(78)91440-7
DO - 10.1016/0006-291X(78)91440-7
M3 - Article
C2 - 208540
AN - SCOPUS:0017890444
VL - 81
SP - 928
EP - 935
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -