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Biochemical studies on the H-2K mutant B6.C-H-2bm10

✍ Scribed by Larry R. Pease; Bruce M. Ewenstein; Diane McGovern; Roger W. Melvold; Tosiki Nisizawa; Stanley G. Nathenso


Publisher
Springer-Verlag
Year
1983
Tongue
English
Weight
677 KB
Volume
17
Category
Article
ISSN
0093-7711

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Biochemical studies of H-2K antigens fro
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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

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## Abstract The B6.C‐H‐2^bm12^ has been examined serologically with a new set of reagents and several complementation studies were performed to determine the extent of the mutation. The results show that: (a) the mutation has also affected the site(s) bound by xenogeneic anti‐Ia antibodies; (b) the

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The C.B6-H-2 dins mutant strain was derived from a spontaneous gain+loss mutation recovered in a (BALB/cKh x C57BL/6Kh)F 1 female (CB6F1). It was backcrossed repeatedly to the BALB/cKh strain for ten generations before being made homozygous and has been maintained by brother x sister matings since.