The activity of collagenase and certain lysosomal hydrolases (cathepsin B1, cathepsin D, beta-glucuronidase and beta-N-acetyl glucosaminidase) was studied in serum and tissues of rats with streptozotocin- or alloxan-induced diabetes. The activity of serum lysosomal enzymes was increased in both grou
Specific radioimmunoassay of glucitol-lysine — application to lens proteins in streptozotocin-diabetic rats
✍ Scribed by M. Yano; F. Hashimoto; M. Sato; C. Ohboshi; M. Hirota; I. Oshima; Y. Ohe; S. Shin; K. Shima
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 429 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0012-186X
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✦ Synopsis
A radioimmunoassay using antibody against glucitol-lysine was developed to quantitate glycated proteins in the lens of diabetic rats. The amount of glycated protein was expressed as molar equivalents of reduced glycated hippuryl lysine (GlcRED-Hip-Lysine). Significant differences (p less than 0.01) were found in the amounts of glycated protein in the lenses of rats with streptozotocin-induced diabetes (3.92 +/- 0.59 nmol/mg protein, n = 5), those with streptozotocin-induced diabetes treated with insulin (2.94 +/- 0.36 nmol/mg protein, n = 4) and normal rats (1.23 +/- 0.22 nmol/mg protein, n = 5). There was a significant correlation between the concentration of glycated protein in the lens and the HbA1c level at the end of the 12 week experiment (r = 0.957, p less than 0.001). These results indicate that glycation of lens protein is parallel with the severity of diabetes in rats.
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