There is a significant relationship between selectivity of proteinuria and tubulointerstitial damage. Moreover, the selectivity of proteinuria has a predictive value on functional outcome. When proteinuria is highly selective, the tubulointerstitial damage is rather infrequent, and 100% of patients develop clinical remission. When proteinuria is moderately selective or nonselective, increasing numbers of patients develop tubulointerstitial damage; in these patients, the functional outcome and response to therapy is partly dependent on tubulointerstitial involvement, and the best predictor of functional outcome is the combination of SI and FE alpha1m.

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Recently we have presented an electrophoretic comparison of genetically determined human serum albumin variants from diverse populations, distinguishing 20 different types of 'monomeric' variants as well as three 'dimeric' variants (Weitkamp et al. 1973; Weitkamp & Neel, 1972). A t this time we compare the 20 previously described types of monomeric variants with 30 more variants, generally rare, and extend our data and conclusions on the population distribution of albumin variants. MATERIALS AND METHODS Each albumin variant, its source, and ethnic origin are listed in the Appendix. Many of the new variants were found in several individuals in a single family. In other cases the variants were found in one or more individuals in a single village. The electrophoretic comparisons were made in the three starch-gel systems, acetate-EDTA a t pH 5.0, tris-lithium-succinate-citrate a t pH 6.0 and tris-EDTA-borate a t pH 6.9, used previously (Weitkamp et al. 1973). RESULTS The results of the comparison of 30 new or recently described serum albumin variants with 20 variants previously distinguished using three starch-gel electrophoretic systems are presented in Table 1. Although the amount of separation reported here for the 20 variants previously described differs slightly from the earlier results, due to minor variations in electrophoretic conditions, the conclusions regarding their mobility relative to normal albumin and to each other remain the same. Three new variants, RS I, Xavante, and Yanomama-2, all slowly migrating, have been identified. Electropherograms showing these variants adjacent to variants with similar mobility are presented in Fig. 1. Albumin RS I, found in an indigene from Somali, has been mentioned in two previous reports. Porta et al. (1972) found it (identified as R.s.) indistinguishable from SO/BS on cellulose acetate electrophoresis a t pH 9-25. The sample available a t the time of our prior comparison (Weitkamp et al. 1973) was sufficiently degraded, as determined by the smeared patterns in the pH 6.0 and 6.9 systems and the altered mobility of normal albumin in the pH 5.0 system, to preclude determination of its mobility. In the present sample, both the normal and variant albumin bands stain less intensely with Amido Black 1OB than the albumin bands