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S S Mandel

Publications and source records attributed to S S Mandel.

3 recordsLinked to original sources

Analysis of spine motion variability using a computerized goniometer compared to physical examination. A prospective clinical study.

A prospective clinical study was carried out to determine whether the CA-6000 Spine Motion Analyzer was more reliable in measuring spine motion compared to previously described methods of physical examination. One-hundred-twenty age-controlled patients with a negative back history were tested with the CA-6000 to establish normal values. Interexaminer and intraexaminer correlation coefficients and coefficients of variation were determined for 30 patients by three different examiners, each testing the patients three times each. Each test consisted of examining flexion, extension, lateral flexion, and rotation. For flexion, the CA-6000 was compared to the double inclinometer and Schober methods. For extension and lateral flexion, the CA-6000 was compared to the double inclinometer and Moll methods. For rotation, the CA-6000 was compared to the double inclinometer method. The interexaminer and intraexaminer variability using the CA-6000 was significantly less (P < or = 0.025) than other methods for all motions except flexion. In flexion, the differences were not significantly different. The data from this experiment indicate that the CA-6000 has significantly less variability in measuring spine motion clinically than the other methods tested.

Adult↗

Increased glycosylation of human lens epithelial basement membrane in diabetes mellitus.

We studied the nonenzymatic glycosylation of lens epithelial basement membranes (LEBM) of senile cataractous lenses of both diabetic and nondiabetic patients. The human LEBMs were isolated from surgically removed senile cataracts and purified by osmotic lysis and detergent treatments. Glycosylation assay of LEBMs was done using the colorimetric method of Flückiger and Winterhalter. The glycosylation value ranged from 16.39 to 92.56 n mol/mg protein overall, with a mean of 63.54 +/- 24.56 n mol/mg protein for the diabetic specimens and a mean of 29.97 +/- 14.48 n mol/mg protein for the nondiabetic controls (P = 0.009). The study confirms our previous observation of in vivo glycosylation of the LEBM and further establishes that diabetic patients have a twofold increase in the amount of LEBM glycosylation when compared to their nondiabetic counterparts.

Aged↗

Glycosylation in vivo of human lens capsule (basement membrane) and diabetes mellitus.

Glycosylation represents a nonenzymatic posttranslational modification of some proteins in vivo. We have investigated possible glycosylation, in vivo, of human lens capsule (basement membrane of lens epithelium) using a colorimetric method. Our study reveals, for the first time, in vivo glycosylation of human lens capsule. Furthermore, the glycosylation of the lens capsule in the diabetics (57.30 +/- 11.26 n moles/mg. protein) is found to be significantly greater than that in their nondiabetic counterparts (29.11 +/- 4.90 n moles/mg. protein) (p less than 0.0005). The present observation represents the first example of increased glycosylation of a basement membrane in the diabetic patients as compared to the nondiabetic controls.

Basement Membrane↗