X-ray scattering study of hagfish protease inhibitor, a protein structurally related to complement and .alpha.2-macroglobulin
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00245a029
Reference49 articles.
1. Limulus α2-macroglobulin. First evidence in an invertebrate for a protein containing an internal thiol ester bond
2. The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
3. The electrophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin molecule
4. Changes of the proteinase binding properties and conformation of bovine .alpha.2-macroglobulin on cleavage of thio ester bonds by methylamine
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1. Evolution of effectors and receptors of innate immunity;Developmental & Comparative Immunology;2001-10
2. The Hagfish Immune System;The Biology of Hagfishes;1998
3. Small-angle scattering study of α1 inhibitor III from rat blood plasma;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1994-08
4. Comparison of conformational changes of pregnancy zone protein and human α2-macroglobulin, a study using hydrophobic affinity partitioning;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1993-07
5. Complement-like protein from the phylogenetically primitive vertebrate,Eptatretus Stouti, is a Humoral Opsonin;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1992-10
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