Literature DB >> 564709

Chemical modification of the arginines in transferrins.

T B Rogers, T Børresen, R E Feeney.   

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Year:  1978        PMID: 564709     DOI: 10.1021/bi00599a026

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


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  7 in total

1.  Structure of human lactoferrin at 3.2-A resolution.

Authors:  B F Anderson; H M Baker; E J Dodson; G E Norris; S V Rumball; J M Waters; E N Baker
Journal:  Proc Natl Acad Sci U S A       Date:  1987-04       Impact factor: 11.205

2.  Egg-white and blood-serum proteins functioning by noncovalent interactions: studies by chemical modification and comparative biochemistry.

Authors:  R E Feeney; D T Osuga
Journal:  J Protein Chem       Date:  1988-12

3.  Arginyl residues are involved in the transport of Fe2+ through the plasma membrane of the mammalian reticulocyte.

Authors:  M González-Sepúlveda; M T Núñez
Journal:  J Membr Biol       Date:  1994-09       Impact factor: 1.843

Review 4.  Arginyl residues and anion binding sites in proteins.

Authors:  J F Riordan
Journal:  Mol Cell Biochem       Date:  1979-07-31       Impact factor: 3.396

5.  Evidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver.

Authors:  S Ramakrishna; W B Benjamin
Journal:  Biochem J       Date:  1981-06-01       Impact factor: 3.857

6.  Human lactotransferrin: molecular, functional and evolutionary comparisons with human serum transferrin and hen ovotransferrin.

Authors:  J Mazurier; M H Metz-Boutigue; J Jollès; G Spik; J Montreuil; P Jollès
Journal:  Experientia       Date:  1983-02-15

7.  Carbonic anhydrase modification for carbon management.

Authors:  Anand Giri; Deepak Pant
Journal:  Environ Sci Pollut Res Int       Date:  2019-12-03       Impact factor: 4.223

  7 in total

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