Series of sequential polypeptides containing lysine or arginine: Preparation and characterization

1988 ◽  
Vol 53 (1) ◽  
pp. 145-156 ◽  
Author(s):  
Jana Pírková ◽  
Svetlana Churkina ◽  
Vladimír Gut ◽  
Ivo Frič ◽  
Karel Bláha
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Average Molecular Weight ◽  
Basic Amino Acid ◽  
Cd Spectra ◽  
Active Esters ◽  
Marked Tendency

The sequential polypeptides (Lys-Ala)n, (Lys-Ala-Ala)n, (Lys-Ala-Ala-Ala)n, (Lys-Leu-Ala)n, (Lys-Leu-Ala-Ala)n, (Lys-Leu-Ala-Ala-Ala)n, (Lys-Ala-Leu)n, (Lys-Ala-Leu-Ala)n, (Orn-Leu-Ala)n,(Arg-Ala-Ala)n, (Arg-Leu-Ala)n, (Arg-Leu-Ala-Ala)n, (Arg-Ala-Leu)n, and (Arg-Ala-Leu-Ala)n were synthesized by polymerization of active esters (1-succinimidyl or pentafluorophenyl) of the corresponding Nα-deblocked monomers. The monomers were prepared using the usual methods of peptide synthesis in solution. Upon dialysis, the average molecular weight of the polymer was 6 000-9 000 as determined by sedimentation in ultracentrifuge. Polypeptides, containing leucine in addition to the basic amino acid, showed a marked tendency to aggregation. CD spectra of the products were measured for characterization.

scholarly journals Lysine as a potential low molecular weight angiogen: its clinical, experimental and in-silico validation- A brief study

2016 ◽  
Author(s):  
Debatosh Datta ◽  
Priyanshu Verma ◽  
Anindita Banerjee ◽  
Sujoy Kar ◽  
Tanima Sengupta ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
In Silico ◽  
Metastatic Cancer ◽  
Basic Amino Acid ◽  
Low Molecular Weight ◽  
Binding Property ◽  
Vegf Receptor ◽  
Angiogenic Response ◽  
In Silico Studies

AbstractGlobally, the area of angiogenesis is dominated by investigations on anti-angiogenic agents and processes, due to its role in metastatic cancer treatment. Although, the area of ischemic tissue reperfusion is having much bigger demand and foot-mark. Following clinical failure of VEGF (Vascular endothelial growth factor) as a potential agent for induction of a controlled angiogenic response in ischemic tissues and organs, the progress is reasonably quiet as for new low molecular weight (LMW) angiogen molecules and their clinical applications are concerned. Basic amino acid Lysine has been observed to have profound angiogenic property in ischemic tissues, which is controlled, reproducible, time bound and without any accompanying reperfusion damage. In this study, the basic amino acid Lysine has been suggested as a LMW-angiogen, where it has been proposed to have a molecular binding property between VEGF and VEGF receptor (VEGFR). Here, the molecular adhesive hypothesis is being probed and confirmed both in the clinical and lab conditions through induced angiogenic response in tissue repair and in chick chorio allantoic membrane (CAM), respectively; and in dry-docking experiments (in-silico studies).

Dimedone (5,5-Dimethylcyclohexane-1,3-dione) as a protecting agent for amino groups in peptide synthesis

1964 ◽  
Vol 17 (11) ◽  
pp. 1282 ◽  
Author(s):  
B Halpern ◽  
LB James
Keyword(s):  
Amino Acid ◽  
Peptide Synthesis ◽  
Amino Acid Esters ◽  
Protecting Group ◽  
Amino Groups ◽  
Active Esters ◽  
Optically Pure ◽  
Derivatives Of ◽  
Protected Peptides ◽  
Acid Esters

The reaction of dimedone (5,5-dimethylcyclohexane-1,3-dione) with amino-acid "active" esters leads to optically pure enamine derivatives. The dimedone derivatives of amino acid esters could also be converted by way of their hydrazides to the corresponding azides. The thiophenyl ester and azide derivatives have been used directly for peptide synthesis. The protecting group can easily be removed from the N-protected peptides by means of aqueous bromine, with the formation of 2,2-dibromodimedone and the hydrobromide of the corresponding peptide ester.

scholarly journals 3-Methylhistidine in actin and other muscle proteins

1967 ◽  
Vol 105 (1) ◽  
pp. 361-370 ◽  
Author(s):  
P. Johnson ◽  
C I Harris ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Basic Amino Acid ◽  
Adult Rabbit ◽  
Muscle Actin ◽  
Muscle Proteins ◽  
Heavy Meromyosin ◽  
Tryptic Digest ◽  
Peptide Fraction

1. By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine has been detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. 2. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. 3. Rabbit skeletal-muscle actin has a 3-methylhistidine:histidine ratio 1:7·6, indicating a minimum molecular weight of 47600. 4. Adult rabbit myosin contains approximately 2 3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.

Amino Acid Sequence of the Small Subunit of Ribulose-1,5-Bisphosphate Carboxylase from Spinach

1979 ◽  
Vol 6 (3) ◽  
pp. 401
Author(s):  
P.G Martin
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Average Molecular Weight ◽  
Small Subunit ◽  
Bisphosphate Carboxylase ◽  
N Terminus ◽  
Proline Substitution ◽  
Ribulosebisphosphate Carboxylase

The complete amino acid sequence of the small subunit of ribulosebisphosphate carboxylase from spinach has been determined. There are 120 amino acids. The N-terminus of the protein is frequently blocked. There is a tyrosine-proline substitution at position 91 and the average molecular weight of the two forms is 13 897. The interest of the sequence data for students of physiology and evolution is discussed.

scholarly journals Virtual 2-D map of the fungal proteome

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tapan Kumar Mohanta ◽  
Awdhesh Kumar Mishra ◽  
Adil Khan ◽  
Abeer Hashem ◽  
Elsayed Fathi Abd-Allah ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Isoelectric Point ◽  
Synonymous Codon ◽  
Average Molecular Weight ◽  
Protein Sequences ◽  
Bimodal Distribution ◽  
Fungal Proteome ◽  
Fungal Kingdom ◽  
Abundant Amino Acid

AbstractThe molecular weight and isoelectric point (pI) of the proteins plays important role in the cell. Depending upon the shape, size, and charge, protein provides its functional role in different parts of the cell. Therefore, understanding to the knowledge of their molecular weight and charges is (pI) is very important. Therefore, we conducted a proteome-wide analysis of protein sequences of 689 fungal species (7.15 million protein sequences) and construct a virtual 2-D map of the fungal proteome. The analysis of the constructed map revealed the presence of a bimodal distribution of fungal proteomes. The molecular mass of individual fungal proteins ranged from 0.202 to 2546.166 kDa and the predicted isoelectric point (pI) ranged from 1.85 to 13.759 while average molecular weight of fungal proteome was 50.98 kDa. A non-ribosomal peptide synthase (RFU80400.1) found in Trichoderma arundinaceum was identified as the largest protein in the fungal kingdom. The collective fungal proteome is dominated by the presence of acidic rather than basic pI proteins and Leu is the most abundant amino acid while Cys is the least abundant amino acid. Aspergillus ustus encodes the highest percentage (76.62%) of acidic pI proteins while Nosema ceranae was found to encode the highest percentage (66.15%) of basic pI proteins. Selenocysteine and pyrrolysine amino acids were not found in any of the analysed fungal proteomes. Although the molecular weight and pI of the protein are of enormous important to understand their functional roles, the amino acid compositions of the fungal protein will enable us to understand the synonymous codon usage in the fungal kingdom. The small peptides identified during the study can provide additional biotechnological implication.

The Structure of Radiation Cross-Linked Poly (ethylene oxide) Gels

1971 ◽  
Vol 29 ◽  
pp. 76-77
Author(s):  
C. E. Cluthe ◽  
G. G. Cocks
Keyword(s):  
Molecular Weight ◽  
Ethylene Oxide ◽  
Parallel Plate ◽  
Average Molecular Weight ◽  
Radical Reaction ◽  
Free Radical Reaction ◽  
Nitrogen Gas ◽  
Poly Ethylene Oxide ◽  
Poly Ethylene ◽  
Initial Viscosity

Aqueous solutions of a 1 weight-per cent poly (ethylene oxide) (PEO) were degassed under vacuum, transferred to a parallel plate viscometer under a nitrogen gas blanket, and exposed to Co60 gamma radiation. The Co60 source was rated at 4000 curies, and the dose ratewas 3.8x105 rads/hr. The poly (ethylene oxide) employed in the irradiations had an initial viscosity average molecular weight of 2.1 x 106.The solutions were gelled by a free radical reaction with dosages ranging from 5x104 rads to 4.8x106 rads.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

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