To characterize the autoantigen of Goodpasture's (anti-glomerular basement membrane) disease, a molecule of 26-kD reactive with autoantibodies from patients' sera was purified from collagenase digests of sheep glomerular basement membrane. Short internal amino acid sequences were obtained after tryptic or cyanogen bromide cleavage, and used to deduce redundant oligonucleotides for use in the polymerase chain reaction on cDNA derived from sheep renal cortex. Molecules of 175 bp were amplified and found to come from two cDNA sequences. One was identical to that of a type IV collagen chain (a5) cloned from human placenta and shown to be expressed in human kidney. The other was from a type IV collagen chain with close similarities to al and a5 chains, and was used to obtain human cDNA sequences by cDNA library screening and by further polymerase chain reaction amplifications.

A multivariate comparison was made among 67 recurrent, past-recurrent, and nonrecurrent dreamers. The participants twice completed measures of psychological well-being, and they also collected a 14-day sample of their own remembered dreams. Multivariate and discriminant analyses showed that recurrent dreamers scored low on psychological well-being and reported more negative dream content. Past-recurrent dreamers scored high on psychological well-being and reported more positive dream content. A single psychometric dimension, which we call psychological well-being, discriminated among the three groups over the entire set of psychological well-being and dream content variables. The results support analytical psychology theory's assertion of the relation between dreaming and psychological adaptation.This study was completed in partial fulfillment of the requirements for the doctoral degree at McGill University by Ronald Brown under the supervision of Don C. Donderi.

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The heterogeneity of antibody as determined by a variety of physical, chemical~ and biological methods has been well established. Since the demonstration of high molecular weight horse antipneumococcal antibody (1), numerous studies have shown electrophoretic, ultracentrifugal, and chromatographic differences in human and various animal antibodies (2, 3). Generally rabbit and human anfi-erythrocyte antibodies are characterized as electrophoreticaUy slow migrating w-globulin of low molecular weight (7S) and low anionic binding, and fast migrating ~,-globulin of high molecular weight (19S) and high anionic binding (2, 3). Although most studies have been restricted to anticellular antibodies, Wassermann antibodies (4), skin-sensitizing antibodies (5), rheumatoid factor (6), and anti-thyroid auto-antibodies (7), have been shown to belong to the high molecular weight class of antibodies. Certain of these antibodies have been associated with the duration of immunization. For example, 19S horse anti-pneumococcal antibody formed early in immunization is followed by the production of low molecular weight antibody on prolonged antigenic stimulation (8). More recently Stelos (9) has reported early rabbit hemolysin to be mostly a ~-1 with a sedimentation rate of 19S and that a 3,-2 hemolysin associated with 6S protein to appear later in immunization. Employing partition chromatography, Porter (10) and Humphrey and Porter (11) found in the early stages of production that anti-protein rabbit antibodies were in the slow moving fractions, and that on further immunization antibody appeared in faster moving fractions. There is, however, a dearth of information of this kind with regard to antibodies to soluble protein antigens. The present study describes the electrophoretic, ultracentrifugal, and chromatographic separation of early and hyperimmune rabbit anti-bovine serum albumin antisera employing the passive hemagglutination (HA) method. Evidence is presented that rabbit anti-protein antibodies are similar to anti-cellular antibodies with respect to their sequential synthesis.