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T3754

Sigma-Aldrich

L-Tyrosine

reagent grade, ≥98% (HPLC)

Synonym(s):

(S)-2-Amino-3-(4-hydroxyphenyl)propionic acid, 3-(4-Hydroxyphenyl)-L-alanine

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About This Item

Linear Formula:
4-(HO)C6H4CH2CH(NH2)CO2H
CAS Number:
60-18-4
Molecular Weight:
181.19
Beilstein:
392441
EC Number:
200-460-4
MDL number:
MFCD00002606
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
24900164
NACRES:
NA.26

grade

reagent grade

Quality Level

200

Assay

≥98% (HPLC)

form

powder

color

white to off-white

mp

>300 °C (dec.) (lit.)

solubility

1 M HCl: soluble 50 mg/mL

application(s)

detection

SMILES string

N[C@@H](Cc1ccc(O)cc1)C(O)=O

InChI

1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1

InChI key

OUYCCCASQSFEME-QMMMGPOBSA-N

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Application

L-Tyrosine has been used to prepare tyrosine solution for tyrosinase assay. It has also been used to assay pepsin activity.

Biochem/physiol Actions

L-Tyrosine is a non-essential amino acid with a polar side chain. It is utilized by cells to synthesize proteins that have a role in signal transduction. L-Tyrosine is a proteogenic amino acid that acts as a receiver of phosphate groups that are transferred by kinases.

Other Notes

Amino acid precursor of dopamine and other catecholamines

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
BCCG7329
BCCF3115
0000109296
0000085907
0000085894

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Study of Physiochemical Parameters for Optimizing Tyrosinase Activity in Rhodococcus ruber C4 and Pseudomonas geniculata C7/C10
Sapna S. Ingle
Journal of Pharmacy Research, 9(6) (2015)
Effect of insoluble fiber supplementation applied at different ages on digestive organ weight and digestive enzymes of layer-strain poultry
J. S. Yokhana
Poultry Science, 95(3), 550-559 (2016)
Karen Timberlake
Chemistry, An Introduction to General, Organic, and Biological Chemistry (2016)
John W Hill
Chemistry for Changing Times (2016)
Keisuke Saito et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(19), 7690-7695 (2013-04-20)
Using quantum mechanics/molecular mechanics calculations and the 1.9-Å crystal structure of Photosystem II [Umena Y, Kawakami K, Shen J-R, Kamiya N (2011) Nature 473(7345):55-60], we investigated the H-bonding environment of the redox-active tyrosine D (TyrD) and obtained insights that help
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Articles

Enzymatic Assay of Proteinase K with Hemoglobin Substrate

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Enzymatic Assay of Proteinase K with Hemoglobin Substrate

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Protocols

Enzymatic Assay of Proteinase K (EC 3.4.21.64)

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

Enzymatic Assay of Protease Using Casein As a Substrate

To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate.

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