CLINICAL-APPLICATIONS OF ELECTROPHORESIS OF HUMAN SALIVARY PROTEINS

被引:23
作者
BEELEY, JA
机构
[1] Oral Biochemistry Unit (Oral Biology Group), University of Glasgow Dental School, Glasgow, G2 3JZ
来源
JOURNAL OF CHROMATOGRAPHY-BIOMEDICAL APPLICATIONS | 1991年 / 569卷 / 1-2期
关键词
D O I
10.1016/0378-4347(91)80233-3
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Human salivary proteins have been studied by electrophoresis in denaturing and non-denaturing polyacrylamide gel electrophoresis (PAGE) as well as by isoelectric focusing (IEF) and two-dimensional procedures, and the clinical applications of this have been reviewed. Whilst non-denaturing PAGE is useful in studying polymorphisms, sodium dodecylsulphate PAGE appears to be otherwise preferable. Immobilized pH gradients containing carrier ampholytes (CAs) give better resolution than CA-based IEF and overcome the problems of cathode drift and loss of basic material. Proline-rich proteins stain poorly with conventional procedures and special techniques are necessary. In clinical studies, findings must be viewed over and above the large number of polymorphisms which occur normally. Studies relating salivary protein and peptide profiles to dental caries susceptibility are encouraging. Specific protein abnormalities have been associated with connective tissue disorders and could form the basis of new non-invasive diagnostic procedures. Protein differences associated with cystic fibrosis and diabetes mellitus, however, merit reinvestigation with the new procedures now available. Detection of HIV antigens in saliva is a new area of research. In the light of new techniques available and new information which has arisen from DNA studies, future prospects for the clinical applications of electrophoresis of saliva look good.
引用
收藏
页码:261 / 280
页数:20
相关论文
共 139 条
[91]   ESSENTIAL PROBLEMS IN QUANTIFICATION OF PROTEINS FOLLOWING COLLOIDAL STAINING WITH COOMASSIE BRILLIANT BLUE DYES IN POLYACRYLAMIDE GELS, AND THEIR SOLUTION [J].
NEUHOFF, V ;
STAMM, R ;
PARDOWITZ, I ;
AROLD, N ;
EHRHARDT, W ;
TAUBE, D .
ELECTROPHORESIS, 1990, 11 (02) :101-117
[92]  
NOLAN A, 1991, J DENT RES, V70, P685
[93]   IMMUNOLOGICAL CROSS-REACTIVITY OF ANIONIC PROTEINS FROM CARIES-FREE AND CARIES-ACTIVE SALIVAS WHICH DIFFER IN BIOLOGICAL PROPERTIES TOWARD ORAL STREPTOCOCCI [J].
OBENAUF, SD ;
COWMAN, RA ;
FITZGERALD, RJ .
INFECTION AND IMMUNITY, 1986, 51 (02) :440-444
[94]   HUMAN-PAROTID SALIVA PROTEIN-COMPOSITION - DEPENDENCE ON PHYSIOLOGICAL FACTORS [J].
OBERG, SG ;
IZUTSU, KT ;
TRUELOVE, EL .
AMERICAN JOURNAL OF PHYSIOLOGY, 1982, 242 (03) :G231-G236
[95]  
OFARRELL PH, 1975, J BIOL CHEM, V250, P4007
[96]  
PAREKH RB, 1988, BRIT J RHEUMATOL, V27, P162
[97]   FUNGISTATIC AND FUNGICIDAL ACTIVITY OF HUMAN-PAROTID SALIVARY HISTIDINE-RICH POLYPEPTIDES ON CANDIDA-ALBICANS [J].
POLLOCK, JJ ;
DENEPITIYA, L ;
MACKAY, BJ ;
IACONO, VJ .
INFECTION AND IMMUNITY, 1984, 44 (03) :702-707
[98]  
PORTER SR, 1987, MED SCI RES-BIOCHEM, V15, P1251
[99]   OLIGOSACCHARIDE STRUCTURES OF THE LOW-MOLECULAR-WEIGHT SALIVARY MUCIN FROM A NORMAL INDIVIDUAL AND ONE WITH CYSTIC-FIBROSIS [J].
REDDY, MS ;
LEVINE, MJ ;
PRAKOBPHOL, A .
JOURNAL OF DENTAL RESEARCH, 1985, 64 (01) :33-36
[100]   PROTEIN TRANSFER FROM ISOELECTRIC-FOCUSING GELS - THE NATIVE BLOT [J].
REINHART, MP ;
MALAMUD, D .
ANALYTICAL BIOCHEMISTRY, 1982, 123 (02) :229-235