Biochemical studies of H-2K antigens from a group of related mutants. II. Identification of a shared mutation in B6-H-2bm6, B6.C-H-2bm7, and B6.C-H-2bm9

✍ Scribed by Karen M. Yamaga; Gertrude M. Pfaffenbach; Larry R. Pease; Diane McGovern; Tosiki Nisizawa; Roger W. Melvold; Henry I. Kohn; Stanley G. Nathenson

• Publisher: Springer-Verlag
• Year: 1983
• Tongue: English
• Weight: 692 KB
• Volume: 17
• Category: Article
• ISSN: 0093-7711
• DOI: 10.1007/bf00364287

✦ Synopsis

In an earlier paper, we presented evidence that two independent mutants of the b9 series, B6-H-2 bin5 (binS) and B6-H-2 b'nl 6 (bin16) carry identical mutations such that tyrosine at residue number 116 of the H-2K b molecule from the parent strain C57BL/6Kh is replaced by a phenylalanine in each of the two mutant molecules. In this paper, we demonstrate, using similar techniques, that the independent b9 series mutants B6-H-2 b"6 (bin6), B6.C-H-2 bin7 (bin7), and B6.C-H-2 bin9 (bin9), which share biological properties with bin5 and bml 6, can be grouped together because they share two identical mutations, one of which is common to bm5 and bml6, a Tyr to Phe interchange at residue number 116. In addition, a second mutation is at residue number 121, where a Cys in the H-2K molecule from B6 is substituted with an Arg in the mutant. Since all of the bg series mutants arose independently and share biological and biochemical characteristics, it is anticipated that study of these mutants could lead to some understanding of the high mutation rate in the K b molecule.