Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function

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Expression of recombinant human mast cell chymase with Asn-linked glycans in glycoengineered Pichia pastoris.

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Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function

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Human enteropeptidase light ch ...... ions of structure and function

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Human enteropeptidase light ch ...... ions of structure and function

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Human enteropeptidase light ch ...... ions of structure and function

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Human enteropeptidase light ch ...... ions of structure and function

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David A Johnson

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Eliot T Smith

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Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide

X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex

Crystal structure of a supercharged variant of the human enteropeptidase light chain

On the size of the active site in proteases. I. Papain

Malabsorption and growth failure due to intestinal enterokinase deficiency

Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase

Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain

Enterokinase (enteropeptidase): comparative aspects

The preparation and properties of bovine enterokinase

Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli

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577-585

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scholarly article

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10.1002/PRO.2239

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2013-03-26T00:00:00Z

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23436726

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3649259

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Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function

about

P2860

P2860

Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function

description

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P2093

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