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The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
After CNBr cleavage of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, five peptides and free homoserine were isolated (see preceding paper in this journal). The amino acid sequences of the three smallest peptides, viz. CB3, CB4 and CB5, were determined by automated Edman degradation and analysis of enzymatic subdigests. These peptides form a continuous stretch of 110 residues from the N terminus: (Formula: See Text).
PMID: 6780353 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Differences in glycosylation pattern of human secretory ribonucleases.
Beintema JJ, Blank A, Schieven GL, Dekker CA, Sorrentino S, Libonati M.
Biochem J. 1988 Oct 15; 255(2):501-5.
[Biochem J. 1988]
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Antibodies against synthetic peptides of herpes simplex virus type 1 glycoprotein D and their capability to neutralize viral infectivity in vitro.
Weijer WJ, Drijfhout JW, Geerligs HJ, Bloemhoff W, Feijlbrief M, Bos CA, Hoogerhout P, Kerling KE, Popken-Boer T, Slopsema K.
J Virol. 1988 Feb; 62(2):501-10.
[J Virol. 1988]
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Structural properties and reactivity of N-terminal synthetic peptides of herpes simplex virus type 1 glycoprotein D by using antipeptide antibodies and group VII monoclonal antibodies.
Bosch DL, Geerligs HJ, Weijer WJ, Feijlbrief M, Welling GW, Welling-Wester S.
J Virol. 1987 Nov; 61(11):3607-11.
[J Virol. 1987]