EurekaMag.com logo
+ Site Statistics
References:
47,893,527
Abstracts:
28,296,643
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

The function of the histidine transfer rna iso accepting species in hemo globin synthesis


, : The function of the histidine transfer rna iso accepting species in hemo globin synthesis. Journal of Biological Chemistry 253(17): 5964-5970

Rabbit reticulocytes contained 2 RNA isoaccepting species for histidine as resolved by various chromatographic methods, while rabbit liver contains only one. These isoacceptors cannot be distinguished by coding properties, consistent with the 'Wobble Hypothesis'. Their function in Hb synthesis in reticulocyte lysates was investigated. Each of the tRNA isoacceptors of reticulocytes and the tRNA species of liver can incorporate histidine into positions in Hb encoded by both of the histidine code words, CAC and CAU. Each can incorporate histidine into all of the histidine-containing positions of Hb. Even in experiments where probably the 2 histidine tRNA species of reticulocytes are placed together in a lysate and are in competition with each other, each incorporates histidine into all of the histidine-containing positions. There is no evidence by either of the tRNA species. The 2 species are attached to reticulocyte ribosomes in the same proportion as they occur in the reticulocyte, also suggesting that neither of them is used preferentially in Hb synthesis. The 1st of the 2 reticulocyte histidine isoacceptors and the histidine tRNA of rabbit liver contain Q base.


Accession: 006680473

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Godeau, J.F.; Beuzard, Y.G.; Cacheleux, J.; Brizard, C.P.; Gibaud, A.; Rosa, J., 1976: Association of hemo globin saint etienne alpha 2 beta 2 92f8 histidine replaced by glutamine with hemo globin a and hemo globin f synthesis and subunit exchange in vitro. The unstable Hb Sainte Etienne (.alpha.2.beta.292F8 His.fwdarw.Gln) (.beta.SE) was found in the red blood cells of an 8-yr-old boy. The composition of this Hb was 26% Saint Etienne [SE], 52% A, 3% A2 and 19% HbF. Studies of Hb synthesis indicated...

Ukita T., 1973: Transfer of valine into rabbit hemo globin from various iso accepting species of valyl transfer rna differing in codon recognition. European Journal Of Biochemistry: 489-496

Yang W.K.; Hilse K.M.; Popp R.A., 1969: Iso accepting transfer rnas and in vitro hemo globin synthesis in c 3 h and c 57 bl mice abstract. Federation Proceedings 28(2): 349

Rudloff E.; Hilse K., 1971: Properties of iso accepting species of lysine transfer rna from rabbit reticulocytes in codon recognition and in hemo globin biosynthesis in vitro. European Journal of Biochemistry 24(2): 313-320

Imai, K.; Adair, G.S., 1977: A simple method for calculating the fractional population of deoxy hemo globin oxy hemo globin and intermediate molecular species of hemo globin as a function of oxygen saturation. The fractional population of molecular species of Hb [human] at various stages of oxygenation can be calculated from O2 equilibrium curve as a function of O2 saturation without knowing values of all the 4 individual equilibrium constants. The calc...

Shih T B.; Jones R.T.; Bonaventura J.; Bonaventura C.; Schneider R.G., 1984: Involvement of histidine hc 3 146 beta in the bohr effect of human hemo globin studies of native and n ethyl maleimide treated hemo globin a and hemo globin cowtown. The involvement of the COOH-terminal histidines of the .beta. chains of human Hb in the allosteric mechanism of O2 binding was studied. Data presented on the functional properties of native and chemically modified forms of Hb Cowtown (.beta.146 Hi...

Bonaventura, J.; Bonaventura, C.; Amiconi, G.; Tentori, L.; Brunori, M.; Antonini, E., 1975: Allo steric interactions in non alpha chains isolated from normal human hemo globin fetal hemo globin and hemo globin abruzzo beta 143 h 21 histidine replaced by arginine. Journal of Biological Chemistry 250(16): 6278-6281

Walker, B.K.; Ballas, S.K.; Burka, E.R., 1980: Terminal stages of hemo globin synthesis 2. lack of effect of alpha hemo globin and beta hemo globin chains on the rate of globin synthesis in a human cell free system. The influence of heme containing .alpha.A and .beta.S globin chains on the rate of synthesis of globin subunits was studied in a human cell-free system derived from sickle reticulocytes. The autologous lysate system produced measurable amounts of...

H.C.; Davis D.G.; Mock N.H.; Lindstrom T.R.; Charache S., 1970: Nmr studies of hemo globin part 4 the structure function relationship of human adult hemo globin a and hemo globin chesapeake and its implication to the nature of oxygenation of hemo globin. Biochemical & Biophysical Research Communications 38(4): 779-786

John M.E.; Waterman M.R., 1980: Structural basis for the conformational states of nitrosyl hemo globin m saskatoon and hemo globin m milwaukee influence of distal histidine residues on proximal histidine iron bonds. The nitrosyl derivatives [human] Hb M Saskatoon (.alpha.2.beta.263 His .fwdarw. Tyr) and M Milwaukee (.alpha.2.beta.267 Val .fwdarw. Glu) were examined to determine the role of these 2 distal amino acid residues in maintaining Hb conformational st...