Literature DB >> 5657452

The isoelectric fractionation of hen's-egg ovotransferrin.

R V Wenn, J Williams.   

Abstract

1. Hen ovotransferrin was examined by isoelectric fractionation. 2. The major component observed in starch-gel electrophoresis can be isolated from the minor component. 3. When non-saturating amounts of iron are added to ovotransferrin, isoelectric fractionation demonstrates the existence of three molecular species corresponding to the metal-free protein, the one-iron-atom-protein complex and the two-iron-atoms-protein complex. 4. Isoelectric fractionation of human serum labelled with (59)Fe suggests that the transferrin of normal human serum also exists as metal-free protein, the one-iron-atom-protein complex and the two-iron-atoms-protein complex. 5. It is concluded that the binding constants for the first and second iron atoms are similar.

Entities:  

Mesh:

Substances:

Year:  1968        PMID: 5657452      PMCID: PMC1198770          DOI: 10.1042/bj1080069

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  14 in total

1.  Genetic polymorphisms in the egg albumen proteins of the domestic fowl.

Authors:  I E LUSH
Journal:  Nature       Date:  1961-03-25       Impact factor: 49.962

2.  Starch gel electrophoresis in a discontinous system of buffers.

Authors:  M D POULIK
Journal:  Nature       Date:  1957-12-28       Impact factor: 49.962

3.  The preparation of crystalline conalbumin.

Authors:  R C WARNER; I WEBER
Journal:  J Biol Chem       Date:  1951-07       Impact factor: 5.157

4.  Purification and properties of human transferrin C and a slow moving genetic variant.

Authors:  W E Roop; F W Putnam
Journal:  J Biol Chem       Date:  1967-05-25       Impact factor: 5.157

5.  Studies on the binding of iron to transferrin and conalbumin.

Authors:  P Aisen; A Leibman; H A Reich
Journal:  J Biol Chem       Date:  1966-04-25       Impact factor: 5.157

6.  The effect of iron addition to avian egg white on the behaviour of conalbumin fractions in starch gel electrophoresis.

Authors:  A Stratil
Journal:  Comp Biochem Physiol       Date:  1967-07

7.  Isoelectric focusing and separation of the subcomponents of lactoperoxidase.

Authors:  A Carlström; O Vesterberg
Journal:  Acta Chem Scand       Date:  1967

8.  On electrophoretic resolution and densitometric determination of apo-transferrin and iron-bound transferrin.

Authors:  R Yoshioka; T Fujii; Y Ito
Journal:  Biochem Biophys Res Commun       Date:  1966-07-20       Impact factor: 3.575

9.  Comparative study of metal-free, iron-saturated and sialic acid-free transferrins.

Authors:  A Bezkorovainy
Journal:  Biochim Biophys Acta       Date:  1966-10-31

10.  A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen.

Authors:  J Williams
Journal:  Biochem J       Date:  1968-06       Impact factor: 3.857

View more
  19 in total

1.  Isoelectric focusing study of radiation damage to dry conalbumin.

Authors:  P Cavatorta; P R Crippa; A M Tosi
Journal:  Experientia       Date:  1978-07-15

2.  Preferential utilization in vitro of iron bound to diferric transferrin by rabbit reticulocytes.

Authors:  E J Zapolski; J V Princiotto
Journal:  Biochem J       Date:  1977-08-15       Impact factor: 3.857

3.  Formation of monoferric ovotransferrins in the presence of chelates.

Authors:  J W Donovan; R A Beardslee; K D Ross
Journal:  Biochem J       Date:  1976-03-01       Impact factor: 3.857

Review 4.  [Isoelectric fractionation in protein chemistry].

Authors:  H E Reis; O Wetter
Journal:  Klin Wochenschr       Date:  1970-06-01

5.  A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen.

Authors:  J Williams
Journal:  Biochem J       Date:  1968-06       Impact factor: 3.857

6.  Iron-binding fragments from the carboxyl-terminal region of hen ovotransferrin.

Authors:  J Williams
Journal:  Biochem J       Date:  1975-07       Impact factor: 3.857

7.  The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis.

Authors:  J Williams
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

8.  A substate-induced conformation change in the reaction of alkaline phosphatase from Escherichia coli.

Authors:  S E Halford; N G Bennett; D R Trentham; H Gutfeund
Journal:  Biochem J       Date:  1969-09       Impact factor: 3.857

9.  Basis of plasma iron exchange in the rabbit.

Authors:  H Huebers; D Uvelli; A Celada; B Josephson; C Finch
Journal:  J Clin Invest       Date:  1982-10       Impact factor: 14.808

10.  The iron-binding properties of hen ovotransferrin.

Authors:  J Williams; R W Evans; K Moreton
Journal:  Biochem J       Date:  1978-08-01       Impact factor: 3.857

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.