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J. Biol. Chem., Vol. 263, Issue 16, 7472-7477, Jun, 1988
FG Oppenheim, T Xu, FM McMillian, SM Levitz, RD Diamond, GD Offner and RF Troxler
Histatins 1, 3, and 5 from human parotid secretion were isolated by gel
filtration on Bio-Gel P-2 and reverse phase high performance liquid
chromatography. The complete amino acid sequences of histatins determined
by automated Edman degradation of the proteins, Staphylococcus aureus V8
protease, and tryptic peptides, are as follows: (Sequence: see text).
Histatins 1, 3, and 5 contain 38, 32, and 24 amino acid residues, have
molecular weights of 4929, 4063, and 3037, respectively, and contain 7
residues of histidine. Histatin 1 contains 1 mol of phosphate/mol of
protein; histatins 3 and 5 lack phosphate. With the exception of Glu
(residue 4) and Arg (residue 11) in histatin 1, the first 22 amino acid
residues of all three histatins are identical, and the carboxyl-terminal 7
residues of histatins 1 and 3 are also identical. The sequence,
-Glu-Phe-Pro-Phe-Tyr-Gly-Asp-Tyr- Gly- (residues 23-29), in histatin 1 is
absent in histatin 3; and the sequence, -Gly-Tyr-Arg- (residues 23-25), in
histatin 3 is absent in histatin 1. The complete sequence of histatin 5 is
contained within the amino terminal 24 residues of histatin 3. The
structural data suggest that histatins 1 and 3 are derived from different
structural genes, whereas histatin 5 is a proteolytic product of histatin
3. All three histatins exhibit the ability to kill the pathogenic yeast,
Candida albicans.
Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
Department of Oral Biology, Goldman School of Graduate Dentistry, Boston, Massachusetts.
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E. J. Helmerhorst, R. F. Troxler, and F. G. Oppenheim The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species PNAS, December 4, 2001; 98(25): 14637 - 14642. [Abstract] [Full Text] [PDF]
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