Bovine P2 protein: sequence at the NH2-terminal of the protein.

Abstract:

:Sequence data from key fragments of the P2 protein established the order of cyanogen bromide (CNBr) peptides in the structure of the protein and the primary structure for approximately one-half of the molecule. Data were obtained from the three tryptic peptides of blocked NH2-terminal CNBr peptide (CN3), the large CNBr peptide of P2 protein (CN1), and a fragment obtained from P2 by cleavage at tryptophan with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine. This last fragment was found to contain an over-lapping sequence that proved the juxtaposition of CN1 and CN3 in P2 protein. Thus, based on this fact and the characteristics of the CNBr peptides, the P2 structure is composed of CNBr peptides in the order: CN3-CN1-CN2(Val)-CN2(Lys). A comparison was made between the partial sequence of P2 protein and the equivalent portion of the structure of bovine myelin basic protein. The structures of these two proteins were found to be distinctly different although certain similarities are found.

journal_name

J Neurochem

authors

Weise MJ,Hsieh DL,Levit S,Brostoff SW

doi

10.1111/j.1471-4159.1980.tb06276.x

subject

Has Abstract

pub_date

1980-08-01 00:00:00

pages

388-92

issue

2

eissn

0022-3042

issn

1471-4159

journal_volume

35

pub_type

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