𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Occupancy of the iron-binding sites of human transferrin in sera obtained from different anatomical sites

✍ Scribed by Vogel, W. ;Herold, M. ;Margreiter, R. ;Bomford, A.

Publisher
Springer-Verlag
Year
1989
Tongue
English
Weight
716 KB
Volume
67
Category
Article
ISSN
1432-1440

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Evidence of conformational changes in th
Evidence of conformational changes in the non-equivalent binding sites of human serum transferrin
✍ P.J. Marsden; F.A. Smith; R.W. Evans πŸ“‚ Article πŸ“… 1989 πŸ› Elsevier Science βš– 671 KB

Samples of monoferric human serum transferrin have been prepared in which the iron occupies predominantly the N-site (sample A) and the C-site (sample B). 111In was then added in concentrations small enough to ensure that there was always an excess of specific binding sites. Because of the presence

Site I on human albumin: Differences in
Site I on human albumin: Differences in the binding of (R)- and (S)-warfarin
✍ Carlo Bertucci; Alessandra Canepa; Giorgio A. Ascoli; Luis F. Lopes Guimaraes; G πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 129 KB

The binding of drugs known to interact with area I on human serum albumin (HSA) was investigated using a chiral stationary phase obtained by anchoring HSA to a silica matrix. In particular, this high-pressure affinity chromatography selector was employed to study the binding properties of the indivi

Identification of functioning regulatory
Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone
✍ P. A. J. Huber; C. S. Redwood; N. D. Avent; M. J. A. Tanner; S. B. Marston πŸ“‚ Article πŸ“… 1993 πŸ› Springer Netherlands 🌐 English βš– 861 KB

A partial clone of caldesmon, coding for the C-terminal 288 amino acids, was isolated from a human fetal liver cDNA library and sequenced. Expression of the clone in Escherichia coli produced a peptide called H1 (M r 32 549), which inhibited tropomyosin-enhanced actomyosin Mg2+-ATPase activity by 90