Abstract:
:Sodium- and potassium-activated adenosinetriphosphatase (Na+, K+-ATPase) purified from dog kidney outer medulla was examined by polyacrylamide gel electrophoresis and by photoaffinity labeling with N-(ouabain)-N'-(2-nitro-4-azidophenyl)-ethylenediamine (NAP-ouabain). The large subunit band (alpha-band) split into two bands on the gel after the enzyme was heat-treated in the presence of 1% sodium dodecylsulfate (SDS). Of the two bands (alpha I and alpha II), alpha I had the same electrophoretic mobility as the original band, while alpha II moved slightly faster. Total conversion into alpha II was not observed, about half of the original remaining as alpha I. Below 60 degree C, heat treatment did not produce alpha II. Phenylmethylsulfonyl fluoride did not prevent the appearance of alpha II. Both alpha I and alpha II were labeled with [3H]NAP-ouabain. Nonspecific incorporation of [3H]NAP-ouabain also occurred irrespective of illumination, but it was removed either by diffusion during staining and destaining of the gel or by treatment of the enzyme with trichloroacetic acid. It is tentatively concluded that the splitting of the band reflects some intrinsic differences in situ of the alpha-subunit of dog kidney membrane Na+,K+-ATPase.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Ohta T,Kawamura M,Hasegawa T,Ishikura H,Nagano Kdoi
10.1093/oxfordjournals.jbchem.a133713subject
Has Abstractpub_date
1982-01-01 00:00:00pages
97-105issue
1eissn
0021-924Xissn
1756-2651journal_volume
91pub_type
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1982-08-01 00:00:00
abstract::A new arginine derivative, N-benzyloxycarbonyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide hydrochloride (ZPVAPA.HCl) was synthesized by the condensation of N-benzyloxy-carbonyl-L-phenylalanyl-L-valine and L-arginine-p-nitroanilide dihydrochloride using dicyclohexylcarbodiimide as a coupling reagent and 1-hydroxy...
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a135018
更新日期:1984-12-01 00:00:00
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pub_type: 杂志文章
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更新日期:1978-08-01 00:00:00
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更新日期:1985-10-01 00:00:00
abstract::We previously isolated a Ca2+-binding protein from a ciliate, Tetrahymena, and designated it as TCBP (Tetrahymena Ca2+-binding protein). The present paper reports that TCBP, which has two high affinity Ca2+-binding sites (Kd=4.6 X 10(-6) M), could activate porcine brain cyclic nucleotide phosphodiesterase at a concent...
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pub_type: 杂志文章
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更新日期:1981-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:1998-03-01 00:00:00
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journal_title:Journal of biochemistry
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pub_type: 杂志文章
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