Short communicationFunctional activities and nonenzymatic glycosylation of plasma proteinase inhibitors in diabetes
References (16)
- et al.
Glycosylation of serum albumin: elevated glycosyl-albumin in diabetic patients
FEBS Lett
(1979) - et al.
Reduced trypsin binding capacity of α2-Macroglobulin in diabetes
Clin Chim Acta
(1986) - et al.
Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation
Biochim Biophys Acta
(1984) Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies
Anal Biochem
(1966)- et al.
Antithrombin (heparin cofactor) assay with ‘new’ chromogenic substrates
Thromb Res
(1977) - et al.
Nonenzymatically glycosylated serum proteins in diabetes mellitus, an index of short-term glycaemia
Diabetologia
(1981) - et al.
Decreased antithrombin III activity in diabetes may be due to nonenzymatic glycosylation
A preliminary report. Thromb Haemostas
(1983) - et al.
Nonenzymatic glycosylation reduces antithrombin III activity
Thromb Haemostas
(1984)
Cited by (20)
Biofluid Proteases Profiling in Diabetes Mellitus
2015, Advances in Clinical ChemistryCitation Excerpt :Thus far, most studies have focused on particular sets of proteases and inhibitors relying on techniques selectively directed to their detection and quantification. Such methodologies include enzyme immunoassay [45,46,48,55,65,67–71,74–78,80], enzyme radiometric assay [63,64], immunoblot [35,37,61,63,85], spectrophotometric/fluorometric methods for determination of protease/inhibitor activity [36,43,44,47,51,56,60,64,66,72,73,81,82,85,86] and other less frequently used techniques such as radioimmunoassay (RIA) [40], nephelometry [54,58], radial immunodiffusion [43], and immunoelectrophoresis [57] (Table 3). Overall, immuno-based assays are the most sensitive and specific approaches to qualitatively and quantitatively evaluate proteases and their inhibitors [88,89].
Antigenic and functional levels of alpha-1-antitrypsin in serum during normal and diabetic pregnancy
2003, European Journal of Obstetrics and Gynecology and Reproductive BiologySerum alpha-1-antitrypsin concentration during normal and diabetic pregnancy
2001, European Journal of Obstetrics and Gynecology and Reproductive BiologySpecific activity of α<inf>1</inf>proteinase inhibitor and α<inf>2</inf>macroglobulin in human serum: Application to insulin-dependent diabetes mellitus
1998, Clinical Immunology and ImmunopathologyDifferential effects of heparin and glucose on structural conformation of human α<inf>1</inf> antitrypsin: Evidence for a heparin-induced cleaved form of the inhibitor
1997, Archives of Biochemistry and BiophysicsAlteration of plasma proteinase-antiproteinase system in type 1 diabetic patients. Influence of sex and relationship with metabolic control
1992, Diabetes Research and Clinical Practice