Abstract:
:Activity of the rat liver microsomal vitamin K-dependent carboxylase has been studied at various concentrations of detergent. The activity which could be solubilized by 0.25% Triton X-100 was low but could be greatly increased if vitamin K-deficient rats were given vitamin K a few minutes before they were killed. At higher concentrations of Triton, more activity was solubilized and this effect was not seen. In vitro carboxylation of endogenous microsomal proteins was decreased by 80-90% if vitamin K was administered 1 min before rats were killed, but the amount of assayable prothrombin precursor was decreased by only 20%. Decarboxylated vitamin K-dependent rat plasma proteins were not substrates for the carboxylase and did not influence peptide carboxylase activity significantly. Purified microsomal prothrombin precursors did, however, stimulate carboxylation of peptide substrate and were used as a substrate for the carboxylase in a preparation from precursor depleted vitamin K-deficient rats.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Shah DV,Swanson JC,Suttie JWdoi
10.1016/0003-9861(83)90519-2subject
Has Abstractpub_date
1983-04-01 00:00:00pages
216-21issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(83)90519-2journal_volume
222pub_type
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journal_title:Archives of biochemistry and biophysics
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更新日期:2007-08-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/0003-9861(88)90489-4
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1983-04-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章,评审
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更新日期:2003-12-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/0003-9861(85)90674-5
更新日期:1985-02-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1016/j.abb.2005.09.019
更新日期:2006-04-15 00:00:00
abstract::Human lactase-phlorizin hydrolase [EC 3.2.1.23-3.2.1.62] is a disaccharidase located in the microvillus membrane of small intestinal epithelial cells. The enzyme is synthesized as a precursor protein in the endoplasmic reticulum and in addition to being glycosylated is subsequently proteolytically processed to the mat...
journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1995-11-10 00:00:00