In:
Bioscience, Biotechnology, and Biochemistry, Informa UK Limited, Vol. 80, No. 5 ( 2016-05-03), p. 878-890
Abstract:
The mammalian peripheral stalk subunits of the vacuolar-type H+-ATPases (V-ATPases) possess several isoforms (C1, C2, E1, E2, G1, G2, G3, a1, a2, a3, and a4), which may play significant role in regulating ATPase assembly and disassembly in different tissues. To better understand the structure and function of V-ATPase, we expressed and purified several isoforms of the human V-ATPase peripheral stalk: E1G1, E1G2, E1G3, E2G1, E2G2, E2G3, C1, C2, H, a1NT, and a2NT. Here, we investigated and characterized the isoforms of the peripheral stalk region of human V-ATPase with respect to their affinity and kinetics in different combination. We found that different isoforms interacted in a similar manner with the isoforms of other subunits. The differences in binding affinities among isoforms were minor from our in vitro studies. However, such minor differences from the binding interaction among isoforms might provide valuable information for the future structural-functional studies of this holoenzyme.
Type of Medium:
Online Resource
ISSN:
0916-8451
,
1347-6947
DOI:
10.1080/09168451.2015.1135043
Language:
English
Publisher:
Informa UK Limited
Publication Date:
2016
detail.hit.zdb_id:
2110940-0
SSG:
12
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