Literature DB >> 5417619

Sedimentation of chemically modified chymotrypsin.

K E Neet, S E Brydon.   

Abstract

Mesh：

Substances：

Year:  1970        PMID： 5417619     DOI： 10.1016/0003-9861(70)90345-0

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


× No keyword cloud information.
  3 in total

1.  Modelling of the serine-proteinase fold by X-ray and neutron scattering and sedimentation analyses: occurrence of the fold in factor D of the complement system.

Authors:  S J Perkins; K F Smith; J M Kilpatrick; J E Volanakis; R B Sim
Journal:  Biochem J       Date:  1993-10-01       Impact factor: 3.857

2.  A 13C-n.m.r. investigation of the ionizations within an inhibitor--alpha-chymotrypsin complex. Evidence that both alpha-chymotrypsin and trypsin stabilize a hemiketal oxyanion by similar mechanisms.

Authors:  M D Finucane; E A Hudson; J P Malthouse
Journal:  Biochem J       Date:  1989-03-15       Impact factor: 3.857

3.  Self-association of alpha-chymotrypsin at low ionic strength in the vicinity of its pH optimum.

Authors:  R Tellam; D J Winzor
Journal:  Biochem J       Date:  1977-03-01       Impact factor: 3.857
  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.