TY - JOUR
T1 - Isolation and characterization of six proteins from rabbit parotid saliva belonging to a unique family of proline-rich proteins
AU - Spielman, A. I.
AU - Bennick, A.
PY - 1989
Y1 - 1989
N2 - Proline-rich proteins are major components of salivary secretion from humans, nondashhuman primates, rats, hamsters and rabbits. They are also synthesized in mice in response to chronic stimulation by β agonists. This study seeks to provide an understanding of the structural and genetic relationships within these families of proteins and to determine the possible function of the proline-rich proteins. Rabbit parotid saliva was collected and proline-rich proteins were affinity purified using goat antibodies to human proline-rich proteins. Further purification was achieved by repeated cation exchange chromatography on a Mono S column using a Fast Protein Liquid Chromatography system. Six basic proline-rich proteins were purified. The apparent molecular weights were between 75,000 and 125,000, based on their mobilities in sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Glycine, glutamine (and glutamate) and proline accounted for 79-87% of total amino acids in all proteins, but proline was present in smaller amounts (17-21%) than in proline-rich proteins from other species. All proteins were glycosylated but not phosphorylated. Circular dichroism of two proline-rich proteins, MS7A and MS5B, indicated the absence of secondary structure. The ndashterminal sequences of three proteins electro-eluted after preparative gel electrophoresis were determined. A high degree of similarity was found in various regions of mouse, rat, monkey and human proline-rich proteins. Rabbits thus synthesize constitutively a family of proteins that are immunologically and structurally related to proline-rich proteins from other species.
AB - Proline-rich proteins are major components of salivary secretion from humans, nondashhuman primates, rats, hamsters and rabbits. They are also synthesized in mice in response to chronic stimulation by β agonists. This study seeks to provide an understanding of the structural and genetic relationships within these families of proteins and to determine the possible function of the proline-rich proteins. Rabbit parotid saliva was collected and proline-rich proteins were affinity purified using goat antibodies to human proline-rich proteins. Further purification was achieved by repeated cation exchange chromatography on a Mono S column using a Fast Protein Liquid Chromatography system. Six basic proline-rich proteins were purified. The apparent molecular weights were between 75,000 and 125,000, based on their mobilities in sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Glycine, glutamine (and glutamate) and proline accounted for 79-87% of total amino acids in all proteins, but proline was present in smaller amounts (17-21%) than in proline-rich proteins from other species. All proteins were glycosylated but not phosphorylated. Circular dichroism of two proline-rich proteins, MS7A and MS5B, indicated the absence of secondary structure. The ndashterminal sequences of three proteins electro-eluted after preparative gel electrophoresis were determined. A high degree of similarity was found in various regions of mouse, rat, monkey and human proline-rich proteins. Rabbits thus synthesize constitutively a family of proteins that are immunologically and structurally related to proline-rich proteins from other species.
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U2 - 10.1016/0003-9969(89)90135-0
DO - 10.1016/0003-9969(89)90135-0
M3 - Article
C2 - 2783045
AN - SCOPUS:0024389081
SN - 0003-9969
VL - 34
SP - 117
EP - 130
JO - Archives of Oral Biology
JF - Archives of Oral Biology
IS - 2
ER -