scholarly journals Trypsin-catalysed formation of pig des-(23-63)-proinsulin from desoctapeptide-(B23-30)-insulin

1986 ◽  
Vol 234 (3) ◽  
pp. 665-670 ◽  
Author(s):  
T Kubiak ◽  
D Cowburn
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Receptor Binding ◽  
Amino Acid Analysis ◽  
Peptide Bond ◽  
Dimethyl Sulphoxide ◽  
Tris Buffer ◽  
Binding Ability ◽  
Solvent Systems

Incubation of pig desoctapeptide-(B23-30)-insulin with trypsin in solvent systems consisting of dimethyl sulphoxide, butane-1,4-diol and Tris buffer resulted in the formation of an extra peptide bond between Arg-B22 and Gly-A1 in the DOPI molecule. This DOPI derivative can also be regarded as pig des-(23-63)-proinsulin. The structure of the new, previously unreported, proinsulin analogue was determined on the basis of amino acid analysis, dansylation and digestion with Staphylococcus aureus V8 proteinase. Receptor-binding ability of des-(23-63)-proinsulin was 20% of that of pig desoctapeptide-(B23-30)-insulin and 0.02% of that of pig insulin.

scholarly journals Hydrolysis of the Peptide Bond and Amino Acid Modification with Hydriodic Acid

1971 ◽  
Vol 24 (4) ◽  
pp. 1235 ◽  
Author(s):  
AS Inglis ◽  
PW Nicholls ◽  
CM Roxburgh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Boiling Point ◽  
Amino Acid Analysis ◽  
Peptide Bond ◽  
Hydriodic Acid ◽  
Acid Modification ◽  
Amino Acid Modification ◽  
Hydrolysis Of

Reaction of hydriodic acid with peptides and proteins has been studied. At the boiling point, hydrolysis of the peptide bond, particularly stable bonds linking valine and isoleucine residues, is facile. Several amino acids react with constantboiling hydriodic acid but the only reactions detrimental to the amino acid analysis are the reduction of serine with concomitant formation of alanine, and the destruction of tryptophan. Gentler conditions of hydrolysis with diluted hydriodic acid are required for analysis of serine. Good results for analysis of proteins for amino acids may be obtained after a 6-hr hydrolysis period.

ChemInform Abstract: TRIS(HYDROXYMETHYL)AMINOMETHANE (TRIS) BUFFER AND AMINO ACID ANALYSIS

1974 ◽  
Vol 5 (19) ◽  
pp. no-no
Author(s):  
GREGORY C. GIBBONS ◽  
STEFFEN STROEBAEK ◽  
ERLING AA. GEERTSEN
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Tris Buffer

scholarly journals Bovine ß-Lactoglobulin E, F and G of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

1981 ◽  
Vol 34 (2) ◽  
pp. 133 ◽  
Author(s):  
K Bell ◽  
HA McKenzie ◽  
DC Shaw
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Tryptic Peptide ◽  
Bos Taurus ◽  
Peptide Mapping ◽  
Northern Territory ◽  
Aureus Strain ◽  
Residue Substitution ◽  
Additional Charge

An electrophoretic examination is made of samples of milk from eight Bali (banteng) cattle, Bos (Bibos) javanicus, in the Northern Territory of Australia. There are two new electrophoretically distinct bovine ft-Iactoglobulins, designated E and F, present in these samples. It is shown by amino acid analysis and tryptic peptide mapping of isolated samples that: (I) both E and F differ from the B variant of domestic cattle (Bos taurus) by + 1 G1y, -1 Glu at residue 157 or 158; and (2) the F variant has the additional charge differences from E and B due to + I Tyr, -1 Asp at residue 129 or 130. It is also shown by studies of peptides produced by the action of Staphylococcus aureus strain V8 protease and by more recent amino acid analyses that (1) the GlyjGlu substitution is at residue 158; (2) there is an additional Bali variant, designated ft-lactoglobulin G, differing from E by + 1 Met, -1 lie at residue 78, but having the same mobility as E; and (3) there is an hitherto undetected neutral residue substitution of + 1 Ser, -1 Pro at position 50 in the F variant. The relation of these variants to other known ft-lactoglobulin variants of the Bos genus is discussed.

Eco-Friendly Synthesis of Peptides Using Fmoc-Amino Acid Chlorides as Coupling Agent Under Biphasic Condition

2020 ◽  
Vol 27 ◽  
Author(s):  
Santosh Y. Khatavi ◽  
K. Kantharaju
Keyword(s):  
Amino Acid ◽  
Acid Chloride ◽  
Acid Ester ◽  
Analytical Techniques ◽  
Peptide Bond ◽  
Amino Acid Ester ◽  
Acid Chlorides ◽  
Peptide Bond Formation ◽  
Green Protocol ◽  
Additional Base

Background: Agro-waste derived solvent media act as a greener process for the peptide bond formation using Nα - Fmoc-amino acid chloride and amino acid ester salt with in situ neutralization and coupling under biphasic condition. The Fmoc-amino acid chlorides are prepared by the reported procedure of freshly distilled SOCl2 with dry CH2Cl2. The protocol found many added advantages such as neutralization of amino acid ester salt and not required additional base for the neutralization, and directly coupling take place with Fmoc-amino acid chloride gave final product dipeptide ester in good to excellent yields. The protocol occurs with complete stereo chemical integrity of the configuration of substrates. Here, we revisited Schotten-Baumann condition, instead of using inorganic base. Objective: To develop green protocol for the synthesis of peptide bond using Fmoc-amino acid chloride with amino acid esters salt. Methods: The final product isolated is analyzed in several spectroscopic and analytical techniques such as FT-IR, 1H-, 13CNMR, Mass spectrometry and RP-HPLC to check stereo integrity and purity of the product. Conclusion: The present method developed greener using natural agro-waste (lemon fruit shell ash) derived solvent medium for the reaction and not required chemical entity.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

scholarly journals The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus

1967 ◽  
Vol 242 (20) ◽  
pp. 4736-4751
Author(s):  
Hiroshi Taniuchi ◽  
Christian B. Anfinsen ◽  
Ann Sodja
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Extracellular Nuclease

scholarly journals Genetic Variation and Evolution of the 2019 Novel Coronavirus

2021 ◽  
pp. 1-13
Author(s):  
Salvatore Dimonte ◽  
Muhammed Babakir-Mina ◽  
Taib Hama-Soor ◽  
Salar Ali
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Rapid Evolution ◽  
Single Amino Acid ◽  
Angiotensin Converting Enzyme 2 ◽  
New Type ◽  
Amino Acid Mutations ◽  
Host Infection ◽  
Human Coronaviruses ◽  
Novel Coronavirus

<b><i>Introduction:</i></b> SARS-CoV-2 is a new type of coronavirus causing a pandemic severe acute respiratory syndrome (SARS-2). Coronaviruses are very diverting genetically and mutate so often periodically. The natural selection of viral mutations may cause host infection selectivity and infectivity. <b><i>Methods:</i></b> This study was aimed to indicate the diversity between human and animal coronaviruses through finding the rate of mutation in each of the spike, nucleocapsid, envelope, and membrane proteins. <b><i>Results:</i></b> The mutation rate is abundant in all 4 structural proteins. The most number of statistically significant amino acid mutations were found in spike receptor-binding domain (RBD) which may be because it is responsible for a corresponding receptor binding in a broad range of hosts and host selectivity to infect. Among 17 previously known amino acids which are important for binding of spike to angiotensin-converting enzyme 2 (ACE2) receptor, all of them are conservative among human coronaviruses, but only 3 of them significantly are mutated in animal coronaviruses. A single amino acid aspartate-454, that causes dissociation of the RBD of the spike and ACE2, and F486 which gives the strength of binding with ACE2 remain intact in all coronaviruses. <b><i>Discussion/Conclusion:</i></b> Observations of this study provided evidence of the genetic diversity and rapid evolution of SARS-CoV-2 as well as other human and animal coronaviruses.

Sign in / Sign up

Export Citation Format

Share Document