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.

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.

Fragmentation of Actin by Thrombin-Like Snake Venom Proteases

1979 ◽  
Author(s):  
M. Hauck ◽  
L. Muszbek
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Snake Venom ◽  
Time Course ◽  
Peptide Bond ◽  
Muscle Actin ◽  
Sds Page ◽  
End Groups ◽  
Bothrops Marajoensis ◽  
Bothrops Moojeni

It has been demonstrated that thrombin can split skeletal muscle actin (Muszbek and Laki, PNAS 1974,71,2208). In the present paper the effect of thrombin-like snake venom proteases (Ancrod and Batroxobins of Bothrops moojeni and Bothrops marajoensis) on actin was studied and compared to the thrombic cleavage of this protein. Only EDTA pretreated G and F actin were split by Ancrod, while, Batroxobins hydrolized native G actin, too. The time course of digestion was followed by SDS PAGE. A split product of 37500 m.w. appeared first which was cleaved further resulting in three lower m.w. fragments. The SDS gel pattern of thrombic fragmentation was well distinguishable from those caused by Ancrod and Batroxobins. The first split products of Batroxobin digestion were isolated and by estimating their N-, and C-terminal end groups and amino acid compositions the peptide bond hydrolyzed first was located in the primary structure of actin. It was established that while thrombin split off two actinopeptides (at Arg ( 28)-Ala(29) and Arg ( 39)-His ( 40) from the N-terminal end of the molecule only Arg ( 39)-His ( 40) was cleaved by Batroxobins.

scholarly journals Action of Dinitrophenyl Amino Acids on Skeletal Muscle Proteins

1969 ◽  
Vol 22 (1) ◽  
pp. 205
Author(s):  
RW Burley ◽  
Jean P Robertson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Equilibrium Dialysis ◽  
Total Absorption ◽  
Muscle Proteins ◽  
Heavy Meromyosin ◽  
Skeletal Muscle Myosin ◽  
Skeletal Muscle Proteins ◽  
Sulphydryl Groups ◽  
Muscle Myosin

Isotherms for the total absorption ofbis(2,4-dinitrophenyl)-L-lysine (bis-DNP-lysine) by rabbit skeletal muscle myosin and heavy meromyosin whose sulphydryl groups had been progressively blocked with p-chloromercuribenzoate were measured by equilibrium dialysis in Tris buffers containing potassium chloride.

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).

Isolation and characterization of related cDNA clones encoding skeletal muscle beta-tropomyosin and a low-molecular-weight nonmuscle tropomyosin isoform

1989 ◽  
Vol 9 (1) ◽  
pp. 185-192
Author(s):  
J A Bradac ◽  
C E Gruber ◽  
S Forry-Schaudies ◽  
S H Hughes
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Cdna Library ◽  
Low Molecular Weight ◽  
Cdna Clones ◽  
Protein Coding ◽  
Coding Sequence ◽  
Untranslated Sequence ◽  
Complete Protein

We have isolated and characterized cDNA clones from chicken cDNA libraries derived from skeletal muscle, body wall, and cultured fibroblasts. A clone isolated from a skeletal muscle cDNA library contains the complete protein-coding sequence of the 284-amino-acid skeletal muscle beta-tropomyosin together with 72 bases of 5' untranslated sequence and nearly the entire 3' untranslated region (about 660 bases), lacking only the last 4 bases and the poly(A) tail. A second clone, isolated from the fibroblast cDNA library, contains the complete protein-coding sequence of a 248-amino-acid fibroblast tropomyosin together with 77 bases of 5' untranslated sequence and 235 bases of 3' untranslated sequence through the poly(A) tract. The derived amino acid sequence from this clone exhibits only 82% homology with rat fibroblast tropomyosin 4 and 80% homology with human fibroblast tropomyosin TM30nm, indicating that this clone encodes a third 248-amino-acid tropomyosin isoform class. The protein product of this mRNA is fibroblast tropomyosin 3b, one of two low-molecular-weight isoforms expressed in chicken fibroblast cultures. Comparing the sequences of the skeletal muscle and fibroblast cDNAs with a previously characterized clone which encodes the smooth muscle alpha-tropomyosin reveals two regions of absolute homology, suggesting that these three clones were derived from the same gene by alternative RNA splicing.

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