Prolonged antidiuretic action of vasopressin analogues in relation to their primary structure

1981 ◽  
Vol 46 (8) ◽  
pp. 1850-1855 ◽  
Author(s):  
Jana Škopková ◽  
Pavel Hrbas ◽  
Jiřina Slaninová ◽  
Tomislav Barth
Keyword(s):  
Amino Acids ◽  
Primary Structure ◽  
Peptide Chain ◽  
Amino Group ◽  
Prolonged Action ◽  
Disulphide Bridge ◽  
Vasopressin Analogues ◽  
Antidiuretic Action

The effectiveness of vasopressin analogues with prolonged antidiuretic action was related to their primary structure. Prolonged action was primarily due to the absence of the amino group of cysteine in position 1 of the peptide chain. The carba substitution of the disulphide bridge and introduction of basic homologous amino acids into position 8 contributed in differing degrees to the prolonged action of the analogues. [8-L-Norarginine]deamino vasopressin was the most potent of the analogues compared; its action was 10 times more prolonged than that of dDAVP.

Special transport and neurological significance of two amino acids in a configuration conventionally designated as D.

1994 ◽  
Vol 196 (1) ◽  
pp. 297-305 ◽  
Author(s):  
H N Christensen ◽  
A A Greene ◽  
D K Kakuda ◽  
C L MacLeod
Keyword(s):  
Amino Acids ◽  
Receptor Site ◽  
Amino Group ◽  
Carboxylate Group ◽  
Gamma Aminobutyric Acid ◽  
Imino Group ◽  
Group A ◽  
The Central Nervous System ◽  
Lower Homolog ◽  
Alpha Amino Acid

We point out an ability of certain amino acids to be recognized at a biological receptor site as though their amino group bore, instead of an alpha relationship to a carboxylate group, a beta, gamma or delta relationship to the same or a second carboxylate group. For aspartate, the unbalanced position of its amino group between a pair of carboxylates allows its occasional biorecognition as a beta-rather than as an alpha-amino acid, whereas for proline and its homologs, their cyclic arrangement may allow the imino group, without its being replicated, to be sensed analogously as falling at either of two distances from the single carboxylate group. The greater separation might allow proline to be seen as biologically analogous to gamma-aminobutyric acid. This more remote positioning of the imino group would allow the D-form of both amino acids to present its amino group in the orientation characteristic of the natural L-form. The dual modes of recognition should accordingly be signalled by what appears to be low stereospecificity, actually due to a distinction in the enantiorecognition of the two isomers. Competing recognition for transport between their respective D- and L-forms, although it does not prove that phenomenon, has been shown for proline and, significantly, even more strongly for its lower homolog, 2-azetidine carboxylate. Such indications have so far revealed themselves rather inconspicuously for the central nervous system binding of proline, reviewed here as a possible feature of a role suspected for proline in neurotransmission.

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

scholarly journals The functional importance of the extreme C-terminal tail in the gene 2 organellar Ca2+-transport ATPase (SERCA2a/b)

1994 ◽  
Vol 303 (3) ◽  
pp. 979-984 ◽  
Author(s):  
H Verboomen ◽  
F Wuytack ◽  
L Van den Bosch ◽  
L Mertens ◽  
R Casteels
Keyword(s):  
Amino Acids ◽  
Splice Variant ◽  
Turnover Rate ◽  
Peptide Chain ◽  
Deletion Mutants ◽  
Functional Difference ◽  
Critical Importance ◽  
Transmembrane Segment ◽  
Functional Importance ◽  
Transport Atpase

Ca(2+)-uptake experiments in microsomal fractions from transfected COS-1 cells have revealed a functional difference between the non-muscle SERCA2b Ca2+ pump and its muscle-specific SERCA2a splice variant. Structurally, the two pumps differ only in their C-terminal tail. The last four amino acids of SERCA2a are replaced in SERCA2b by a 49-residue-long peptide chain containing a very hydrophobic stretch which could be an additional transmembrane segment. The functionally important subdomains in the SERCA2b tail were analysed by constructing three SERCA2b deletion mutants lacking 12, 31 or 49 amino acids. The mutants and the parental SERCA2 pumps were expressed in COS-1 cells and analysed for functional difference. SERCA2b had a twofold higher Ca2+ affinity, a twofold lower turnover rate and a 10-fold lower vanadate-sensitivity than SERCA2a and the mutants. Since each of the three truncated versions of SERCA2b acquire the characteristic properties of SERCA2a, it is concluded that the stretch of the last 12 residues of SERCA2b is of critical importance.

scholarly journals Wachstumsgeschwindigkeit der Peptidkette im Tabakmosaikvirus

1967 ◽  
Vol 22 (12) ◽  
pp. 1280-1291 ◽  
Author(s):  
H. Diringer ◽  
F. A. Anderer ◽  
G. Schramm
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Protein Synthesis ◽  
Peptide Chain ◽  
Cell Protein ◽  
Virus Protein ◽  
Animal Cells ◽  
Tobacco Leaves ◽  
Soluble Cell ◽  
C Terminus

The rate of incorporation of labelled amino acids into the complete tobacco mosaic virus (TMV), into soluble virus protein and into soluble cell proteins has been determined in discs of infected and healthy tobacco leaves. The rate of overall protein synthesis is increased by 50% in the infected leaves. At least 60% of the increase derives from the synthesis of virus-specific proteins and the synthesis of cellular proteins is not inhibited. The virus protein synthesis is strongly temperature dependent and shows a maximum at 28 °C.The exchange of free labelled amino acids between the external medium and the inner cellular pool reaches equilibrium within ten minutes. The influence of the exchange rate on the measurement of the kinetics of peptide chain synthesis is discussed in detail.Discs from infected leaves were incubated for short periods at low temperatures in media containing 3H-tyrosine or 3H-proline. Peptides isolated after 5 minutes incubation at 15 °C were found to be uniformly labelled with no apparent gradient of radioactivity from the N- to the C-terminus. The results indicate that the growth rate of the peptide chain at 15 °C is probably higher than 2 - 3 amino acids/sec and at 28 °C higher than 20 amino acids/sec. These values are higher than those for animal cells and similar to those for protein synthesis in Escherichia coli.Comparison of the growth rate of TMV protein with rate of total protein synthesis and the number of ribosomes in the tobacco leaves indicate that only a small portion of the ribosomes takes part in cell protein synthesis.

ChemInform Abstract: 3,5-Dinitro-1-(4-nitrophenyl)-4-pyridone as a Novel Protecting Reagent for the Amino Group in L-Amino Acids. Part 2.

1983 ◽  
Vol 14 (25) ◽  
Author(s):  
E. MATSUMURA ◽  
H. OKA ◽  
N. KAMAKURA ◽  
Y. HEIKE ◽  
M. ARIGA ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Group
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