scholarly journals Effect of Carboxyl-Group of D-Glutamic Acid or γ-Carboxy-D-glutamic Acid as N-Terminal Amino Acid of 111In-Diethylenetriaminepentaacetic Acid-Octreotide on Accumulation of Radioactivity in Kidney

2007 ◽  
Vol 30 (11) ◽  
pp. 2226-2228 ◽  
Author(s):  
Hiromichi Akizawa ◽  
Madoka Saito ◽  
Ikuko Tsukamoto ◽  
Tatsuya Ohkura ◽  
Takaya Shimizu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Carboxyl Group ◽  
Diethylenetriaminepentaacetic Acid ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals ON THE SEROLOGICAL SPECIFICITY OF PEPTIDES

1932 ◽  
Vol 55 (5) ◽  
pp. 781-796 ◽  
Author(s):  
K. Landsteiner ◽  
J. van der Scheer
Keyword(s):  
Amino Acid ◽  
Carboxyl Group ◽  
Enzyme Specificity ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Serological Specificity ◽  
Free Carboxyl ◽  
Glycyl Glycine

With the idea that studies on the serological properties of peptides may ultimately aid in the understanding of the precipitin reactions of proteins, antigens have been prepared containing aminobenzoylated dipeptides, namely glycyl-glycine, glycyl-d, l-leucine, d, l-leucyl-glycine and d, l-leucyl-d, l-leucine. These four antigens were found to be different serologically, their specificity depending on the structure of the terminal amino acid carrying the free carboxyl group, and to a less degree also on the second amino acid. The results were obtained by means of precipitin and inhibition tests. Analogies to observations on enzyme specificity are discussed.

scholarly journals Terminal Amino Groups in Wool and S-Carboxymethyl Kerateine 2

1957 ◽  
Vol 10 (2) ◽  
pp. 225 ◽  
Author(s):  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Total N ◽  
Purified Protein Derivative ◽  
Terminal Residue ◽  
Terminal Amino

The N-terminal residues of Merino 64's quality wool and of a purified protein derivative extracted from it, S-carboxymethyl kerateine 2, have been determined. A similar total N-terminal residue content is present in both wool and S�carboxymethyl kerateine 2 comprising glycine, serine, threoni~e, aspartic acid, glutamic acid, and alanine. These occur in different proportions in the two materials and valine is an additional N-terminal amino acid present only in wool.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

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