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Identification of the Pm and PmS human parotid salivary proteins as basic proline-rich proteins

✍ Scribed by L. C. Anderson; D. L. Kauffman; P. J. Keller

Publisher
Springer
Year
1982
Tongue
English
Weight
329 KB
Volume
20
Category
Article
ISSN
0006-2928

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✦ Synopsis

Amino acid composition and electrophoretic mobility suggest that two polymorphic proteins in human parotid saliva, Pm and ProS, are basic proline-rich proteins. Comparison of two basic proline-rich proteins previously isolated by D. L. Kauffman and P. J. Keller (1979) β€’Arch. Oral. Biol. 24:249], IB-6 and IB-9, with ProS and Pm demonstrated corresponding electrophoretic mobilities on cationic polyacrylamide slab gels. Further, the amino acid compositions o fiB-9 and Pm were found to be similar. Although differences in amino acid composition and carbohydrate content were noted, such differences could be accounted for, suggesting that IB-9 and Pm are identical.

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## Abstract The solid phase synthesis of a 59 amino acid human salivary protein IB7 has been accomplished using Fmoc strategy. Because the protein contains 25 proline, 13 glycine and 9 glutamine residues the coupling time, piperidine delivery and acetic anhydride reaction time were increased. Yield