• Publications
  • Influence
The structure of the lentil (Lens culinaris) lectin. Amino acid sequence determination and prediction of the secondary structure.
The subunit structure and complete amino acid sequence of the lectin extracted from Lens culinaris (LcL) seeds was determined. In previous studies, the primary structure of the alpha-chain (Mr =Expand
  • 92
  • 1
  • Open Access
Image analysis of the heavy form of the acetylcholine receptor from Torpedo marmorata.
The structure of the heavy (H) form of the acetylcholine receptor, which comprises two covalently linked 250,000 Mr oligomers, has been investigated by numerical analysis of electron microscopeExpand
  • 44
  • 1
The structure of BAcillus subtilis levansucrase at 3.8 A resolution.
The tertiary structure of Bacillus subtilis levansucrase (EC at 3.8 A resolution has been obtained from x-ray diffraction data by the method of multiple isomorphous replacements using threeExpand
  • 26
  • 1
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of
The interactions between the catalytic regions of the subunit of the bifunctional enzyme aspartokinase I-homoserine dehydrogenase I, although not necessary for the catalytic functions, are shown toExpand
  • 78
Beef pancreas tryptophanyl-tRNA synthetase. Molecular weight, composition and spectral properties.
The molecular weight of beef pancreatic tryptophanyl-tRNA synthetase has been determined by Sephadex filtration, by equilibrium sedimentation according to Yphantis and to Van Holde and Baldwin, andExpand
  • 31
The subunit structure of tryptophanyl transfer ribonucleic acid synthetase from beef pancreas.
Abstract The subunit structure of tryptophanyl-tRNA synthetase from beef pancreas (mol wt 108,000) has been studied by high speed and low speed equilibrium sedimentation, light scattering, gelExpand
  • 33
Quaternary structure of polynucleotide phosphorylase from Escherichia coli.
Purification of polynucleotide phosphorylase from Escherichia coli by a modified technique yeilds a protein that appears to be homogeneous when analyzed by disc-gel electrophoresis. Two species ofExpand
  • 22