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Michael Richardson

Researcher at Durham University

Publications -  78
Citations -  3770

Michael Richardson is an academic researcher from Durham University. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 35, co-authored 78 publications receiving 3656 citations. Previous affiliations of Michael Richardson include Universidade Federal de Pelotas & Federal University of Ceará.

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The proteinase inhibitors of plants and micro-organisms

TL;DR: Recent advances in knowledge of the proteinase inhibitors of plants and micro-organisms are reviewed and details of the specificity, occurrence and distribution of these proteins are summarized, and modern methods for their isolation, purification and assay are discussed.
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A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds or sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat γ-purothionins

TL;DR: Three isoinhibitors of locust and cockroach gut α‐amylases were purified from seeds of sorghum by saline extraction, precipitation with ammonium sulphate, affinity chromatography on Red‐Sepharose and preparative RP‐HPLC on Vydac C??? to determine the complete primary structures.
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A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor

TL;DR: A maize protein is described which is a potent in vitro inhibitor of bovine trypsin and the α-amylase from Tribolium castaneum beetles and which is highly similar to the intensely sweet protein thaumatin, suggesting a possible function for these proteins.
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Purification and amino acid sequences of six TX3 type neurotoxins from the venom of the Brazilian 'armed' spider Phoneutria nigriventer (keys.)

TL;DR: Six neurotoxic peptides purified from the venom of the spider Phoneutria nigriventer exhibited sequence similarities to one another and to the neurotoxins from the venoms of the spiders Hololena curta and Agelenopsis aperta, which were most evident in the location of the Cys residues.
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The complete amino acid sequence of the bifunctional α‐amylase/trypsin inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)

TL;DR: The complete amino acid sequence of the bifunctional α‐amylase/trypsin inhibitor from ragi seeds was determined by analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide and by digestion with trypsin, chymotrypsin; the S. aureus V8 protease and a Pro‐specific protease.