ChemInform Abstract: The Nitrogenous Hamigerans: Unusual Amino Acid-Derivatized Aromatic Diterpenoid Metabolites from the New Zealand Marine Sponge Hamigera tarangaensis.

ChemInform ◽  
2015 ◽  
Vol 46 (21) ◽  
pp. no-no
Author(s):  
Jonathan D. Dattelbaum ◽  
A. Jonathan Singh ◽  
Jessica J. Field ◽  
John H. Miller ◽  
Peter T. Northcote
Keyword(s):  
New Zealand ◽  
Amino Acid ◽  
Marine Sponge ◽  
Unusual Amino Acid

The Nitrogenous Hamigerans: Unusual Amino Acid-Derivatized Aromatic Diterpenoid Metabolites from the New Zealand Marine Sponge Hamigera tarangaensis

2014 ◽  
Vol 80 (1) ◽  
pp. 304-312 ◽  
Author(s):  
Jonathan D. Dattelbaum ◽  
A. Jonathan Singh ◽  
Jessica J. Field ◽  
John H. Miller ◽  
Peter T. Northcote
Keyword(s):  
New Zealand ◽  
Amino Acid ◽  
Marine Sponge ◽  
Unusual Amino Acid

scholarly journals New Nitrogenous Spongian Diterpenes from the New Zealand Marine Sponge Darwinella Oxeata

2021 ◽  
Author(s):  
◽  
Katie Orlagh Dowle
Keyword(s):  
New Zealand ◽  
Amino Acid ◽  
Cell Line ◽  
Marine Sponge ◽  
Detailed Examination ◽  
Marine Sponges ◽  
Side Chain ◽  
Spectroscopic Techniques ◽  
New Compounds ◽  
Mtt Assays

<p>During the course of this research five New Zealand marine sponges were investigated. Detailed examination of one of the species, Darwinella oxeata, has resulted in the isolation of ten compounds whose structures were elucidated using a variety of spectroscopic techniques and a simple derivatisation reaction. These compounds were identified as rearranged spongian diterpenes with the aplysulphurane backbone. Five of these compounds have been previously reported, though two of them were originally isolated from another marine sponge, Dendrilla membranosa. The five new compounds, oxeatamides C to G (25-29), were found to have the same diterpene portion as the oxeatamides already isolated from this sponge. They do, however, differ in the gamma-lactam side chain, which is proposed to be of amino acid origin. The new oxeatamides showed moderate levels of cytotoxicity against the HL-60 cell line in MTT assays.</p>

scholarly journals New Nitrogenous Spongian Diterpenes from the New Zealand Marine Sponge Darwinella Oxeata

2021 ◽  
Author(s):  
◽  
Katie Orlagh Dowle
Keyword(s):  
New Zealand ◽  
Amino Acid ◽  
Cell Line ◽  
Marine Sponge ◽  
Detailed Examination ◽  
Marine Sponges ◽  
Side Chain ◽  
Spectroscopic Techniques ◽  
New Compounds ◽  
Mtt Assays

<p>During the course of this research five New Zealand marine sponges were investigated. Detailed examination of one of the species, Darwinella oxeata, has resulted in the isolation of ten compounds whose structures were elucidated using a variety of spectroscopic techniques and a simple derivatisation reaction. These compounds were identified as rearranged spongian diterpenes with the aplysulphurane backbone. Five of these compounds have been previously reported, though two of them were originally isolated from another marine sponge, Dendrilla membranosa. The five new compounds, oxeatamides C to G (25-29), were found to have the same diterpene portion as the oxeatamides already isolated from this sponge. They do, however, differ in the gamma-lactam side chain, which is proposed to be of amino acid origin. The new oxeatamides showed moderate levels of cytotoxicity against the HL-60 cell line in MTT assays.</p>

An unusual amino acid sequence of an AL-protein, AL-109, derived from a kappa I chain

Amyloid ◽  
2001 ◽  
Vol 8 (4) ◽  
pp. 274-276 ◽  
Author(s):  
Shucking Wang ◽  
Knut Sletten ◽  
Per Westermark
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Unusual Amino Acid

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Biochemistry ◽  
1978 ◽  
Vol 17 (3) ◽  
pp. 442-445 ◽  
Author(s):  
Mark A. Hermodson ◽  
Kirk C. S. Chen ◽  
Thomas M. Buchanan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Unusual Amino Acid

Hamigerans R and S: Nitrogenous Diterpenoids from the New Zealand Marine Sponge Hamigera tarangaensis

2018 ◽  
Vol 81 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Ethan F. Woolly ◽  
A. Jonathan Singh ◽  
Euan R. Russell ◽  
John H. Miller ◽  
Peter T. Northcote
Keyword(s):  
New Zealand ◽  
Marine Sponge

scholarly journals L-asparaginase: acute effects on protein synthesis in rabbits with normal and increased fibrinogen production

Blood ◽  
1984 ◽  
Vol 63 (4) ◽  
pp. 823-827 ◽  
Author(s):  
BM Alving ◽  
CF Barr ◽  
DB Tang
Keyword(s):  
Protein Synthesis ◽  
New Zealand ◽  
Amino Acid ◽  
Plasma Proteins ◽  
Serum Proteins ◽  
Intravenous Dose ◽  
Single Intravenous Dose ◽  
Acute Effects ◽  
Abnormal Rate ◽  
New Zealand Rabbits

Abstract The acute effects of a single intravenous dose of L-asparaginase on protein synthesis were studied in normal rabbits and in animals that had received turpentine to stimulate fibrinogen production. Male New Zealand rabbits received L-asparaginase (500 U/kg) 16 hr before the injection of the radiolabeled amino acid [75Se]selenomethionine (75SeM). Incorporation of 75SeM into fibrinogen and serum proteins in the L-asparaginase-treated rabbits was the same as for saline-treated controls, with fibrinogen representing approximately 5% of the labeled plasma proteins. In turpentine-treated rabbits, the maximal incorporation of 75SeM into serum proteins remained unchanged, whereas 75SeM-fibrinogen increased sixfold and accounted for 25% of the labeled proteins. Animals that received L-asparaginase at the same time as turpentine or 14 hr later showed significant decreases in synthesis of both serum proteins and fibrinogen. 75SeM-fibrinogen that was purified from L-asparaginase-treated rabbits underwent normal catabolism when injected into normal recipient rabbits. These data indicate that L- asparaginase can acutely cause partial inhibition of both serum protein and fibrinogen synthesis when administered to rabbits shortly before or during a period of increased fibrinogen production. Fibrinogen that is synthesized in the presence of L-asparaginase does not have an abnormal rate of catabolism.

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