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J. Biol. Chem., Vol. 269, Issue 12, 8642-8646, 03, 1994
JM Shin and G Sachs
The gastric H,K-ATPase consists of an alpha, beta heterodimer. To determine
which part of the alpha subunit is associated with the beta subunit, hog
gastric vesicles were trypsinized, which left most of the beta subunit
undigested. The vesicles were solubilized with either C12E8
(polyoxyethylene 8 lauryl ester) or Nonidet P-40 and then passed over a
wheat germ agglutinin column, which retained the beta subunit. Among the
fragments of membrane spanning segments obtained by digestion in the
absence of K+, only one peptide fragment of the alpha subunit coeluted with
the beta subunit, representing only the M7 and M8 membrane spanning
segments of the alpha subunit along with their extracytoplasmic connecting
loop. With K+ present during digestion, the fragments at 19-21 kDa and at
9.4 kDa were retained on the column, representing the M7 to C-terminal end
and the M5/loop/M6 sector of the enzyme. These results provide biochemical
evidence that a region of the alpha subunit containing the M7/loop/M8
sector is bound to the beta subunit under both digestion conditions; but
when the C-terminal 180- amino acid sector of the alpha subunit remains
intact, as found in the presence of K+, there is an additional retention of
the M5/loop/M6 sector of the alpha subunit.
Identification of a region of the H,K-ATPase alpha subunit associated with the beta subunit
Wadsworth Veterans Administration Medical Center, Los Angeles, California.
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