epsilon-Amino-lysine-bound glucose in human tissues obtained at autopsy. Increase in diabetes mellitus.

The level of nonenzymatically epsilon-lysine-bound glucose (NEBG) of tissue proteins obtained at autopsy has been determined with a specific method recently described. The mean values expressed as nmol lysine-bound glucose per mumol phenylalanine were 34 for tendon, 13 for aorta, 16 for coronary artery, 23.5 for femoral nerve, 10 for glomerular basement membrane, and 30 for lung parenchyma for tissues from nondiabetics and 86, 39.5, 34, 60, 29, and 57 for tissues form diabetics, respectively. NEBG was below detection limit in skeletal muscle from either nondiabetic or diabetic subjects. Tendon and aorta NEBG levels correlated well with those from other tissues (r = 0.8-0.94, except r = 0.68 for glomerular basement membrane). A fairly good correlation was also found when NEBG of aorta was compared with the mean blood sugar level determined during the last weeks of hospitalization. Finally, an arbitrary index of diabetic late complication was compared with NEBG of aorta. There appears to be a tendency of an increase of the index of complications along with an increase in tissue glucosylation. The possible role of nonenzymatic glucosylation in the long-term complication of diabetes is discussed.

Partial field-induced magnetic order in the spin-liquid kagomé Nd3Ga5SiO14.

The distorted kagomé system Nd3Ga5SiO14 has been investigated with neutron scattering down to 0.046 K with no evidence of magnetic long range order of the Nd3+ moments in a zero field. Substantial diffuse scattering is observed which is in agreement with nearest-neighbor correlations between the fluctuating spins. Upon the application of a field in the c direction, the diffuse scattering is reduced in intensity while the magnetic Bragg peaks grow in intensity to saturate by 1 T to 1/2 of the expected magnetization. These measurements suggest that a unique spin-liquid state develops in Nd3Ga5SiO14 with a frustration index of f approximately |theta|/T_{C}> or =1300.

Standardization of serum fructosamine assays.

We have calibrated a secondary serum protein standard by use (as primary standards) of samples of albumin and polylysine glycated with [14C]glucose in vitro, the glycation of which was assessed by radioactivity measurements and by elementary analysis for C and N. Using this standard for calibration in our improved fructosamine assay, one obtains an average fructosamine value of 247 mumol/L for nondiabetic individuals (or, in terms of total serum protein, 3.2 mumol/g)--about a tenth the value we obtained when we used the fructosamine assay of Johnson et al. (Clin Chim Acta 1983;127:87-95), standardized with desoxymorpholinofructose. In contrast, results corresponded well with the value for mean glycation of serum proteins, 3 mumol/g, determined by a furosine/HPLC method. Evidently the proposed procedure, in which a standard sharing the binding characteristics of endogenous glycated proteins is used together with our modified new fructosamine assay, leads to more realistic values for the concentrations of glycated serum proteins.