Peptide hemoglobins

The primary structure of a protein is the sequence of residues in the peptide chain. Aspartame consists of phenylalanine (Phe) and aspartic acid (Asp), and so its primary structure is Phe-Asp. Three fragments of the primary structure of human hemoglobin are... 

Hormone response elements (for steroids, T3, retinoic acid, peptides, etc) act as—or in conjunction with— enhancers or silencers (Chapter 43). Other processes that enhance or silence gene expression—such as the response to heat shock, heavy metals (Cd and Zn +), and some toxic chemicals (eg, dioxin)—are mediated through specific regulatory elements. Tissue-specific expression of genes (eg, the albumin gene in liver, the hemoglobin gene in reticulocytes) is also mediated by specific DNA sequences. 

Hemoglobins by Automatic Peptide Chromatography". Cold Spring Harbor Symp. Quant. Biol., (1964), 297. 

Human hemoglobin (< + P) CaMVenhanced 35S promoter/ CaMV 35S terminator Transit peptide of small subunit of RubisCO of Pisum sativum N. tabacum 0.05% of seed protein 37... 

Clinical tests are targeted to measure the concentration of different sets of compounds, such as small molecules (e.g., amino acids, fatty acids, organic acids, steroids) and peptides and proteins (e.g., thyroid stimulating hormone, hemoglobin A 1C) and oligonucleotides (e.g., DNA, RNA, SNPs). The presence, absence, or altered concentrations of a diagnostic compound or compounds may indicate the presence of a disease, type and severity of a disease, risk factors for disease, what is the basis for... 

Guidotti, G., R. J. Hill, and IV. Konigsberg The structure of human hemoglobin. TI. The sepanition and amino acid composition of the tryptic peptides from the a and p chains. Journ. Biol. Chem. 237, 2184-2195 (1962). 

Konigsberg, W., and R. J. Hill The structure ol human hemoglobins. 111. The sequence of amino acid.s in the tryptic peptides of the a-chain. Journ. Biol. Chem. 237, 2517 -2561 (1962). 

The coding sequences of a- and P-globins of human hemoglobin have been fused to the sequence of the chloroplastic transit peptide of the small subunit of Rubisco. These proteins were then coexpressed in transgenic tobacco plants, resulting in the production of a functional form of tetra-meric hemoglobin. The results demonstrate that a complex multimeric protein such as recombinant human hemoglobin can be obtained from tobacco in a functional form. 

Dintzis, H.M. (1961) Assembly of the peptide chains of hemoglobin. Proc. Natl. Acad. Sci. USA 47, 247-261. 

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