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616-07-9

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616-07-9 Usage

General Description

DL-ornithine is a naturally occurring amino acid that is important for the urea cycle, which is responsible for the removal of ammonia from the body. It is often used as a dietary supplement to promote muscle growth, enhance athletic performance, and improve overall health. DL-ornithine is also thought to have potential benefits for reducing fatigue, supporting liver health, and promoting wound healing. It is considered generally safe and well-tolerated, but excessive intake may cause gastrointestinal side effects. Overall, DL-ornithine plays a crucial role in various physiological functions and may offer several potential health benefits as a supplement.

Check Digit Verification of cas no

The CAS Registry Mumber 616-07-9 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 6,1 and 6 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 616-07:
(5*6)+(4*1)+(3*6)+(2*0)+(1*7)=59
59 % 10 = 9
So 616-07-9 is a valid CAS Registry Number.
InChI:InChI=1/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)

616-07-9SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017

1.Identification

1.1 GHS Product identifier

Product name ornithine

1.2 Other means of identification

Product number -
Other names Ornithine

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:616-07-9 SDS

616-07-9Relevant articles and documents

Catenulobactins A and B, Heterocyclic Peptides from Culturing Catenuloplanes sp. with a Mycolic Acid-Containing Bacterium

Hoshino, Shotaro,Ozeki, Masahiro,Awakawa, Takayoshi,Morita, Hiroyuki,Onaka, Hiroyasu,Abe, Ikuro

supporting information, p. 2106 - 2110 (2018/09/12)

The production of two new heterocyclic peptide isomers, catenulobactins A (1) and B (2), in cultures of Catenuloplanes sp. RD067331 was significantly increased when it was cocultured with a mycolic acid-containing bacterium. The planar structures and absolute configurations of the catenulobactins were determined based on NMR/MS and chiral-phase GC-MS analyses. Catenulobactin B (2) displayed Fe(III)-chelating activity and moderate cytotoxicity against P388 murine leukemia cells.

FUNCTIONALIZED FLUORINE CONTAINING PHTHALOCYANINE MOLECULES

-

, (2015/03/16)

Functionalized fluorine containing phthalocyanine molecules, methods of making, and methods of use in diagnostic applications and disease treatment are disclosed herein. In some embodiments, the fluorine containing phthalocyanine molecules are functionalized with a reactive functional group or at least one cancer-targeting ligand (CTL). The CTL can facilitate more efficient binding and/or internalization to a cancer cell than to a healthy cell. The CTL can inhibit expression of oncoprotein in some embodiments. The pthalocyanine moiety can be used in diagnostic applications, such as fluorescence labeling of a cancer cell, and/or treatment applications, such as catalyzing formation of a reactive oxygen species (ROS) which can contribute to cell death of a cancer cell.

Lysine racemase from a lactic acid bacterium, Oenococcus oeni: Structural basis of substrate specificity

Kato, Shiro,Hemmi, Hisashi,Yoshimura, Tohru

, p. 505 - 508 (2013/02/25)

Oenococcus oeni, a lactic acid bacterium, possesses a lysine racemase, which has a specific activity towards basic amino acids. A comparison of amino acid residues around the active site suggested that Ile222 and Tyr354 of the Geobacillus stearothermophilus alanine racemase, which shares 60% sequence similarity with lysine racemase, were replaced by Thr224 and Trp355 in the O. oeni lysine racemase. T224I/W355Y double mutations significantly decreased the activity of lysine racemase, whereas I222T/Y354W double mutations endowed alanine racemase with lysine racemization activity. These results suggest that the two residues play an important role in lysine racemization.

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