scholarly journals Collagen Hydrolysates for Skin Protection: Oral Administration and Topical Formulation

Antioxidants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 181 ◽  
Author(s):  
Gabriel Aguirre-Cruz ◽  
Arely León-López ◽  
Verónica Cruz-Gómez ◽  
Rubén Jiménez-Alvarado ◽  
Gabriel Aguirre-Álvarez
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Oral Administration ◽  
Antioxidant Properties ◽  
Aromatic Amino Acids ◽  
Natural Antioxidants ◽  
Transepidermal Water Loss ◽  
Skin Aging ◽  
Skin Protection ◽  
Topical Formulation

Antioxidants are molecules that delay or inhibit the oxidation of other molecules. Its use significantly increased in recent years in the diet of people. Natural antioxidants are replacing the use of synthetic antioxidant ingredients due to their safety, nutritional, and therapeutic values. Hydrolyzed collagen (HC) is a popular ingredient considered to be an antioxidant. This low molecular weight protein has been widely utilized due to its excellent biocompatibility, easy biodegradability, and weak antigenicity. It is a safe cosmetic biomaterial with good moisturizing properties on the skin. The antioxidant properties of HC are conditioned to the size of the molecule: the lower the molecular weight of peptides, the greater the ability to donate an electron or hydrogen to stabilize radicals. The antioxidant capacity of HC is mostly due to the presence of hydrophobic amino acids in the peptide. The exact mechanism of peptides acting as antioxidants is not clearly known but some aromatic amino acids and histidine are reported to play an important role in the antioxidant activity. Oral ingestion of HC increases the levels of collagen-derived peptides in the blood torrent and improves the skin properties such as elasticity, skin moisture, and transepidermal water loss. Additionally, daily intakes of HC protect the skin against UV melasma, enhances the fibroblast production and extracellular matrix of the skin. HC has been identified as a safe cosmetic ingredient for topical formulations with good moisturizing properties at the stratum corneum layer of the skin. It reduces the effects of skin aging (dryness, laxity, and wrinkles). The use of HC as a principal ingredient in safe formulations for skin protection was reviewed and compared when it is used by topical and/or oral administration.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

Calcium-binding proteins in a vorticellid contractile organelle

1975 ◽  
Vol 19 (1) ◽  
pp. 203-213
Author(s):  
W.B. Amos ◽  
L.M. Routledge ◽  
F.F. Yew
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Sodium Dodecyl ◽  
Aromatic Amino Acids ◽  
Calcium Binding Proteins ◽  
Polyacrylamide Gels ◽  
Protein Species ◽  
Low Concentrations

The proteins of the contractile spasmoneme of Zoothamnium have been examined for comparison with other motile systems. Though capable of calcium-induced contraction, glycerinated preparations of the spasmoneme contain neither actin nor tubulin at levels that can be detected in polyacrylamide gels. Sixty per cent of the protein in sodium dodecyl sulphate gels migrates in a band at a molecular weight of approximately 20,000, consisting largely of 2 similar protein species which are here given the name of spasmins. The amino acid composition of 2 spasmin fractions has been determined by a fluorimetric method. They are rich in Asx, Glx and serine, but have few aromatic amino acids and no cystine or methionine. In calcium-buffered polyacrylamide gels, it was observed that a reduction in the electrophoretic mobility of the spasmins was induced specifically by calcium (but not magnesium) at the same low concentrations as induce contraction. This indicates that the spasmins are calcium-binding proteins which may be involved directly in the calcium-induced contraction of the spasmoneme.

Low Molecular Weight Sunflower Protein Hydrolysate with Low Concentration in Aromatic Amino Acids

1996 ◽  
Vol 44 (4) ◽  
pp. 967-971 ◽  
Author(s):  
Juan Bautista ◽  
Inmaculada Hernandez-Pinzon ◽  
Manuel Alaiz ◽  
Juan Parrado ◽  
Francisco Millan
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Protein Hydrolysate ◽  
Aromatic Amino Acids ◽  
Low Molecular Weight ◽  
Low Concentration ◽  
Sunflower Protein

Free aromatic amino acids in egg yolk show antioxidant properties

2011 ◽  
Vol 129 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Chamila Nimalaratne ◽  
Daise Lopes-Lutz ◽  
Andreas Schieber ◽  
Jianping Wu
Keyword(s):  
Amino Acids ◽  
Antioxidant Properties ◽  
Aromatic Amino Acids ◽  
Egg Yolk

Inhibition of Platelet Aggregation by Dialysable Fibrinogen Degradation Products (FDP)

1970 ◽  
Vol 23 (01) ◽  
pp. 091-098 ◽  
Author(s):  
Jolanta Stachurska ◽  
Z Latałło ◽  
Maria Kopeć
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Platelet Aggregation ◽  
Active Component ◽  
Degradation Products ◽  
Aromatic Amino Acids ◽  
Inhibit Platelet Aggregation ◽  
Molecular Fragments ◽  
Fibrinogen Degradation Products ◽  
Inhibition Of Platelet Aggregation

SummaryDuring prolonged proteolysis of fibrinogen by plasmin dialysable, low molecular fragments accumulate which inhibit platelet aggregation induced by thrombin, ADP, adrenaline and noradrenaline. These fragments isolated by dialysis were separated on sephadex G-25 column. The active component has probably a molecular weight lower than 5,000 and does not contain aromatic amino acids.

scholarly journals Enzymatic Hydrolysis of Broken Rice Protein: Antioxidant Activities by Chemical and Cellular Antioxidant Methods

2021 ◽  
Vol 8 ◽  
Author(s):  
Likun Ren ◽  
Jing Fan ◽  
Yang Yang ◽  
Yue Xu ◽  
Fenglian Chen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Enzymatic Hydrolysis ◽  
Metal Ion ◽  
Sodium Dodecyl ◽  
Antioxidant Properties ◽  
Length Distribution ◽  
Cell Aging ◽  
Rice Protein ◽  
Broken Rice

Excessive reactive oxygen species (ROS) is an important cause of aging, and supplementing antioxidants through diet is one of the important ways to delay aging. Some studies have confirmed that rice protease hydrolysate has antioxidant activity, but was rarely been investigated on cells. Thus, commercial enzymes, alkaline enzyme, neutral enzyme, pepsin, chymotrypsin, and trypsin were selected to hydrolyze broken rice protein (BRP) to obtain the corresponding hydrolysates, which were A-broken rice protein hydrolysate (BRPH), N-BRPH, P-BRPH, C-BRPH, and T-BRPH, respectively. Then the antioxidant properties of BRPHs were evaluated by different chemical and cellular antioxidation. Molecular weight, peptide length distribution, and amino acid sequence were detected to insight into the antioxidant properties. Among BRPHs, the A-BRPH displayed the strongest hydroxyl radical scavenging activity (IC50 = 1.159 mg/ml) and metal ion-chelating activities (IC50 = 0.391 mg/ml). Furthermore, cellular antioxidation confirmed that A-BRPH significantly increased cell viability and inhibited the intracellular ROS release in both aging cells and cell-aging processes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results revealed that peptides with molecular weight <14.5 KDa were produced by enzymatic hydrolysis. Additionally, A-BRPH rich in low molecular weight (<3 kDa) and short-length peptides with some specific amino acids, such as aromatic and hydrophobic amino acids, contributes to the antioxidant properties. This study provided theoretical to the utilization of broken rice and confirmed that A-BRPH could be used in new anti-aging food and health products for human consumption.

scholarly journals The purification and properties of l-histidine-2-oxoglutarate aminotransferase from Pseudomonas testosteroni

1975 ◽  
Vol 147 (2) ◽  
pp. 327-334 ◽  
Author(s):  
A J Hacking ◽  
H Hassall
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Purification And Properties ◽  
Ping Pong ◽  
Purification Scheme ◽  
Low Activity ◽  
Cellulose Column ◽  
Pseudomonas Testosteroni

1. Inducible L-histidine--2-oxoglutarate aminotransferase was purified some 170-fold from extracts of Pseudomonas testosteroni. 2. The preparation showed only one major component after electrophoresis on polyacrylamide gels, though additional minor bands were observed when samples concentrated on a DEAE-cellulose column were used. 3. The molecular weight of the enzyme was found to be approx. 70000 by chromatography on Sephadex G-200. 4. The purification scheme produced enzyme that was inactive in the absence of pyridoxal 5′-phosphate. 5. The equilibrium constant for the reaction L-histidine+2-oxoglutarate equilibrium imidazolylpyruvate+L-glutamate was 0.49. 6. The reaction mechanism was Ping Pong. 7. The enzyme was shown to have only low activity towards aromatic amino acids and was highly specific for 2-oxoglutarate.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

The Efficient Preparation of Radiolabeled Aromatic Amino Acids via Cu-Mediated Radiofluorination using Ni-complexes

2019 ◽  
Author(s):  
A Craig ◽  
N Kolks ◽  
E Urusova ◽  
BD Zlatopolskiy ◽  
B Neumaier
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids
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