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NH 2 ‐TERMINAL ANALYSIS OF WOLFGRAM AND FOLCH‐LEES PROTEOLIPID PROTEINS 1
Author(s) -
Wiggins R. C.,
Valle U. Del,
Joffe S.
Publication year - 1974
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1974.tb07597.x
Subject(s) - glycine , serine , amino acid , lees , alanine , chemistry , chromatography , paper chromatography , lysine , biochemistry , enzyme , fermentation
— The NH 2 ‐terminal amino acids of Wolfgram and Folch‐Lees proteolipids of bovine and human CNS myelin were determined using the cyanate method (S tarke & S myth , 1963) followed by direct amino acid analysis of the products. Glycine predominated in every case and was recovered in amounts similar to the results described by W hikehart & L ees (1973), who used a dansylation technique followed by thin layer chromatography of the DNS‐amino acids. In the present study substantial amounts of glutamic acid, serine, alanine and aspartic acid were also recovered, plus traces of other amino acids. Few differences were observed between Wolfgram and Folch‐Lees proteolipids. The end group products of purified W1 proteolipid of bovine Wolfgram fraction, of diazometholysed Folch‐Lees proteolipid, and of a sample of phosphatidyl serine had essentially the same composition. The similarity of these results, especially for both fractionated and unfractionated Wolfgram proteolipid, may be evidence that the observed products are derived from phosphoglycerides present in proteolipid rather than from the actual NH 2 ‐terminals of the protein.