Synthesis of a Protected Tetrapeptide Amide Containing the Carboxyl Terminal Sequence of Lysine-Vasopressin1

1956 ◽  
Vol 78 (22) ◽  
pp. 5883-5887 ◽  
Author(s):  
Roger Roeske ◽  
F. H. C. Stewart ◽  
R. J. Stedman ◽  
Vincent du Vigneaud
Keyword(s):  
Terminal Sequence ◽  
Carboxyl Terminal ◽  
Protected Tetrapeptide

The amino- and carboxyl-terminal sequence of bovine rhodopsin

1977 ◽  
Vol 6 (4) ◽  
pp. 559-570 ◽  
Author(s):  
Paul A. Hargrave ◽  
Shao-Ling Fong
Keyword(s):  
Terminal Sequence ◽  
Bovine Rhodopsin ◽  
Carboxyl Terminal

Peptides with Carboxyl-Terminal Sequence of Alanine—Proline: Detection by a Human Monoclonal Antibody

Hybridoma ◽  
1995 ◽  
Vol 14 (1) ◽  
pp. 45-50 ◽  
Author(s):  
YOSHIKAZU KIKUMOTO ◽  
TAKANORI OKA ◽  
JIA-NING CAO ◽  
LAN SZE ◽  
REIKO F. IRIE
Keyword(s):  
Monoclonal Antibody ◽  
Human Monoclonal Antibody ◽  
Terminal Sequence ◽  
Carboxyl Terminal

scholarly journals THE AMINO ACID COMPOSITION OF HYPERTENSIN II AND ITS BIOCHEMICAL RELATIONSHIP TO HYPERTENSIN I

1956 ◽  
Vol 104 (2) ◽  
pp. 183-191 ◽  
Author(s):  
Kenneth E. Lentz ◽  
Leonard T. Skeggs ◽  
Kenneth R. Woods ◽  
Joseph R. Kahn ◽  
Norman P. Shumway
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Content ◽  
Amino Acid Content ◽  
Converting Enzyme ◽  
Terminal Sequence ◽  
Carboxyl Terminal ◽  
Hydrolysis Of

Preparations of hypertensin II, obtained from the treatment of hypertensin I by the action of the hypertensin converting enzyme of plasma and purified by countercurrent distribution, were quantitatively analyzed for their amino acid content. Chromatography on ion exchange columns showed the presence of equimolar amounts of aspartic acid, proline, valine, isoleucine, tyrosine, phenylalanine, histidine, and arginine. Hypertensin I was found to contain one mole of leucine and one mole of histidine in addition to the amino acids of hypertensin II. These two amino acids were isolated from the conversion products of hypertensin I and identified as the peptide histidylleucine. Carboxypeptidase digestion of hypertensin I showed the carboxyl terminal sequence of amino acids to be residue-phenylalanyl-histidylleucine. Similar studies of hypertensin II demonstrated residue-phenylalanine. It was concluded that the conversion of hypertensin I by the plasma hypertensin converting enzyme involved hydrolysis of the phenylalanyl-histidine bond to form hypertensin II and histidylleucine. The further removal by carboxypeptidase of phenylalanine from hypertensin II destroyed all of the vasoconstrictor activity.

scholarly journals Recycling of proteins from the Golgi compartment to the ER in yeast.

1990 ◽  
Vol 111 (2) ◽  
pp. 369-377 ◽  
Author(s):  
N Dean ◽  
H R Pelham
Keyword(s):  
Fusion Protein ◽  
Recognition System ◽  
Dependent Manner ◽  
Terminal Sequence ◽  
Yeast Saccharomyces Cerevisiae ◽  
Subcellular Organelles ◽  
Er Retention ◽  
Golgi Compartment ◽  
Carboxyl Terminal

In the yeast Saccharomyces cerevisiae, the carboxyl terminal sequence His-Asp-Glu-Leu (HDEL) has been shown to function as an ER retention sequence (Pelham, H. R. B., K. G. Hardwick, and M. J. Lewis. 1988. EMBO (Eur. Mol. Biol. Organ.) J. 7:1757-1762). To examine the mechanism of retention of soluble ER proteins in yeast, we have analyzed the expression of a preproalpha factor fusion protein, tagged at the carboxyl terminus with the HDEL sequence. We demonstrate that this fusion protein, expressed in vivo, accumulates intracellularly as a precursor containing both ER and Golgi-specific oligosaccharide modifications. The Golgi-specific carbohydrate modification, which occurs in a SEC18-dependent manner, consists of alpha 1-6 mannose linkages, with no detectable alpha 1-3 mannose additions, indicating that the transit of the HDEL-tagged fusion protein is confined to an early Golgi compartment. Results obtained from the fractionation of subcellular organelles from yeast expressing HDEL-tagged fusion proteins suggest that the Golgi-modified species are present in the ER. Overexpression of HDEL-tagged preproalpha factor results in the secretion of an endogenous HDEL-containing protein, demonstrating that the HDEL recognition system can be saturated. These results support the model in which the retention of these proteins in the ER is dependent on their receptor-mediated recycling from the Golgi complex back to the ER.

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