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Immunological Nonidentity of 19K Protein and TP 0 in Peripheral Nervous System Myelin
Author(s) -
Smith Marion Edmonds,
Perret Virginia
Publication year - 1986
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.1471-4159.1986.tb00699.x
Subject(s) - glycoprotein , myelin , nitrocellulose , peripheral nervous system , fucose , biochemistry , myelin basic protein , trypsin , chemistry , in vitro , antibody , microbiology and biotechnology , biology , central nervous system , immunology , enzyme , endocrinology , membrane
Peripheral nervous system myelin contains as the major structural protein a glycoprotein known as P 0 . Another glycoprotein present in smaller amounts, known as the 19K or X protein, has been previously identified as derived from P 0 and identical with the main tryptic degradation product of P 0 (TP 0 ). Although both P 0 and 19K protein incorporated fucose in vitro and stained on polyacrylamide gels with the periodic acid‐Schiff stain for carbohydrate, only the P 0 blotted to nitrocellulose paper showed immunoreactivity to an antibody to P 0 , whereas the 19K protein did not. Furthermore, when P 0 was hydrolyzed with trypsin or elastase, the main degradation products reacted with P 0 on immunoblots, whereas the 19K protein showed no immunoreactivity. From these studies and those of others, it may be concluded that the 19K protein shows some similarities to TP 0 , but probably has a different structure. P 0 and 19K protein do not appear to be related as shown by lack of cross‐immunoreac‐tivity.