β-Amylase Thiol Groups POSSIBLE REGULATOR SITES
Joseph Spradlin,John A. Thoma +1 more
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TLDR
It is proposed that modification of the protein results in a conformation change that is proportional to substituent size, and supported by a demonstration that β-amylase can be reversibly inactivated via disulfide interchanges.About:
This article is published in Journal of Biological Chemistry.The article was published on 1970-01-10 and is currently open access. It has received 56 citations till now. The article focuses on the topics: Iodoacetamide & Active site.read more
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Journal ArticleDOI
Recent developments in understanding the regulation of starch metabolism in higher plants
TL;DR: Recently discovered aspects of the fine control of starch metabolism indicate that a number of key reactions are controlled by post-translational modifications of enzymes, including redox modulation and protein phosphorylation.
Journal ArticleDOI
Redox regulation of carbon storage and partitioning in response to light and sugars
TL;DR: Experimental data will be provided showing that the isozyme from pea leaf chloroplasts is activated by reduced thioredoxin f or m in a similar way, and recent evidence will be discussed showing that key enzymes of de novo fatty acid synthesis and ammonium assimilation are regulated by reversible disulphide-bond formation similar to AGPase.
Book ChapterDOI
6 Plant and Animal Amylases
TL;DR: This chapter outlines the recent developments in the amylase field, with a discussion of the emerging fields of biosynthesis and the control of amylases action, and the simplest and the least desirable alkaline oxidation method.
Journal ArticleDOI
Subunit constitution of proteins: a table.
Journal ArticleDOI
Reaction of protein disulfide groups with Ellman's reagent: A case study of the number of sulfhydryl and disulfide groups in Aspergillus oryzae α-amylase, papain, and lysozyme
TL;DR: Ellman's reagent, 5,5′-dithiobis[2-nitrobenzoic acid] (DTNB) is a standard reagent for the determination of reactive sulfhydryl groups by absorbance measurement at 412 nm and established methods for the fast and accurate determination of the number of sulfHydryl and disulfide groups in proteins.
References
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Journal ArticleDOI
Tissue sulfhydryl groups
TL;DR: A water-soluble (at pH 8) aromatic disulfide [5,5′-dithiobis(2-nitrobenzoic acid] has been synthesized and shown to be useful for determination of sulfhydryl groups.
Journal ArticleDOI
Detection of sugars on paper chromatograms.
TL;DR: Modifications are introduced, based on a test given by Feigl for reducing sugars, which eliminate the heating step, and in which the reagents are applied in organic solvents, thus removing the danger of migration of the sugar spots.
Journal ArticleDOI
Chromatography of Amino Acids on Sulfonated Polystyrene Resins. An Improved System
TL;DR: A systematic study has been made of the separations of amino acids by elution analysis on columns of synthetic ion exchange resins, demonstrating that synthetic resins are capable of separating most of the common amino acids from one another.
Journal ArticleDOI
Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase
TL;DR: Direct physiochemical studies concerning the enzyme aspartate transcarbamylase (ATCase) in terms of its subunit structure and binding of the specific inhibitory metabolite, cytidine triphosphate (CTP), reveal the existence of eight receptor sites on the enzyme.
Journal ArticleDOI
A model for the myosin molecule
TL;DR: A model for the myosin molecule is proposed,based on three equal weight polypeptide chains in the form of a three-stranded α rope, based on X-ray diffraction, light scattering and optical rotatory data.
Related Papers (5)
Competitive Inhibition by Substrate during Enzyme Action. Evidence for the Induced-fit Theory1,2
John A. Thoma,Daniel E. Koshland +1 more