scholarly journals Amino Acid Sequence of a Feather Keratin From Silver Gull (Larus novae-hollandiae) and Comparison with One from Emu (Dromaius novae-hollandiae)

1974 ◽  
Vol 27 (4) ◽  
pp. 369 ◽  
Author(s):  
IJ O'Donnell ◽  
AS Inglis
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tryptic Digestion ◽  
Crystalline Region ◽  
Feather Keratin ◽  
Matrix Region ◽  
Polypeptide Chains ◽  
Selection Of

The amino acid sequence of the major components of the silver gull feather calamus has been determined and compared with that of the emu. The sequenator was used with a modified Edman-Begg program to facilitate determination of the sequence of the large hydrophobic fragment obtained on tryptic digestion. The main features of the comparison were: (1) the overall structures of the polypeptide chains were similar, having non-crystalline cystine-rich sections towards either end of the chain separated by a large crystalline region of 62 residues which contained the majority of the hydrophobic and serine and glycine residues; (2) approximately one-sixth of the residues were different in the two species, with the majority of changes occurring in the tails (i.e. non-crystalline or matrix region). The data argue for stringent demands in the selection of amino acids for the crystalline part of the feather molecule, a severity that is probably comparable to the strict requirements for the sequence of some of the enzymes.

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

scholarly journals Determination of Amino Acid Composition of Ganirelix Acetate in an Injectable Formulation by Pre-column Derivatization with 6-Aminoquinolyl-N-hydroxysuccinimidyl Carbamate

2020 ◽  
Vol 58 (8) ◽  
pp. 687-694
Author(s):  
Kumarswamy Ummiti ◽  
J V Shanmukha Kumar
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Flash Chromatography ◽  
Molar Ratio ◽  
Acid Mixture ◽  
Injectable Formulation

Abstract Ganirelix is a synthetic decapeptide linked with nine different amino acids. To understand the peptide amino acid sequence or primary structure, the first step is to determine the amino acid composition of the peptide which can be a determining factor for the peptide immunogenicity. Edman degradation is not a suitable analytical technique to identify amino acid sequence present in Ganirelix due to the absence of uncharged N-terminal amino group. To address this challenge, a pre-column derivatization method was developed with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent. In the present work, the Ganirelix active pharmaceutical ingredient present in the injectable formulation was isolated by fraction collection and further purified by flash chromatography. The amino acid composition of Ganirelix is assayed by carrying out acid hydrolysis with 6 mol L−1 hydrochloric acid solution containing 1% phenol at 100°C for 24 h and derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent solution, followed by determination of individual amino acids by reverse-phase chromatography using a C18 column. High resolution was achieved for the nine amino acid mixture. The amino acid composition results of temperature-stressed Ganirelix generic product and reference listed drug are in good agreement with the theoretical molar ratio of label information.

scholarly journals Phenotypic, Biochemical, and Genetic Analysis of KPC-41, a KPC-3 Variant Conferring Resistance to Ceftazidime-Avibactam and Exhibiting Reduced Carbapenemase Activity

2019 ◽  
Vol 63 (12) ◽  
Author(s):  
Linda Mueller ◽  
Amandine Masseron ◽  
Guy Prod’Hom ◽  
Tatiana Galperine ◽  
Gilbert Greub ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Genetic Analysis ◽  
Amino Acid Sequence ◽  
Cloning And Expression ◽  
Content Type ◽  
Amino Acid Insertion

ABSTRACT A novel KPC variant, KPC-41, was identified in a Klebsiella pneumoniae clinical isolate from Switzerland. This β-lactamase possessed a 3-amino-acid insertion (Pro-Asn-Lys) located between amino acids 269 and 270 compared to the KPC-3 amino acid sequence. Cloning and expression of the blaKPC-41 gene in Escherichia coli, followed by determination of MIC values and kinetic parameters, showed that KPC-41, compared to those of KPC-3, has an increased affinity to ceftazidime and a decreased sensitivity to avibactam, leading to resistance to ceftazidime-avibactam once produced in K. pneumoniae. Furthermore, KPC-41 exhibited a drastic decrease of its carbapenemase activity. This report highlights that a diversity of KPC variants conferring resistance to ceftazidime-avibactam already circulate in Europe.

Amino acid sequence and d/l-configuration determination of peptides utilizing liberated N-terminus phenylthiohydantoin amino acids

1998 ◽  
Vol 813 (2) ◽  
pp. 267-275 ◽  
Author(s):  
Takayuki Iida ◽  
Hirokazu Matsunaga ◽  
Tomofumi Santa ◽  
Takeshi Fukushima ◽  
Hiroshi Homma ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
N Terminus

scholarly journals Purification of feline lysosomal α-mannosidase, determination of its cDNA sequence and identification of a mutation causing α-mannosidosis in Persian cats

1997 ◽  
Vol 328 (3) ◽  
pp. 863-870 ◽  
Author(s):  
Thomas BERG ◽  
K. Ole TOLLERSRUD ◽  
U. Steven WALKLEY ◽  
Donald SIEGEL ◽  
Øivind NILSSEN
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Reverse Transcriptase ◽  
Cdna Sequence ◽  
Molecular Heterogeneity ◽  
Lysosomal Storage ◽  
Reverse Transcriptase Pcr ◽  
Pcr Products

α-Mannosidosis is a lysosomal storage disorder that is caused by the deficiency of lysosomal α-mannosidase. Feline α-mannosidosis is a well-characterized animal model used for studying pathological and therapeutic aspects of lysosomal storage disorders. We here report the purification of feline liver lysosomal α-mannosidase and determination of its cDNA sequence. The active enzyme consisted of three polypeptides, with molecular masses of 72, 41 and 12 kDa, joined by non-covalent forces. The cDNA sequence of feline lysosomal α-mannosidase was determined from reverse transcriptase PCR products obtained from skin fibroblast mRNA. The deduced amino acid sequence contained the N-terminal sequences of the 72 and 41 kDa peptides. This indicated that the enzyme is synthesized as a single-chain precursor with a putative signal peptide of 50 amino acids followed by a polypeptide chain of 957 amino acids, which is cleaved into the three polypeptides of the mature enzyme. The deduced amino acid sequence was 81.1 and 83.2% identical with the human and bovine lysosomal α-mannosidases sequences respectively. A 4 bp deletion was identified in an α-mannosidosis-affected Persian cat by DNA sequencing of reverse transcriptase PCR products. The deletion resulted in a frame shift from codon 583 and premature termination at codon 645. No lysosomal α-mannosidase activity could be detected in the liver of this cat. A domestic long-haired cat expressing a milder α-mannosidosis phenotype than the Persian cat had a lysosomal α-mannosidase activity of 2% of normal. This domestic long-haired cat did not possess the 4 bp deletion, proving molecular heterogeneity for feline α-mannosidosis.

The Croonian Lecture, 1966 - The genetic code

1967 ◽  
Vol 167 (1009) ◽  
pp. 331-347 ◽  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleic Acid ◽  
Amino Acid Sequence ◽  
Genetic Code ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Standard Set ◽  
Polypeptide Chains

Genes are made of nucleic acid. Enzymes are made of protein. The amino acid sequence of a particular protein is synthesized under instruction from a particular piece of nucleic acid. Each protein is made of one or more polypeptide chains, synthesized by condensing together amino acids, head to tail, with the elimination of water. A typical polypeptide chain is several hundred amino acid residues long. Nevertheless only twenty different kinds of amino acids are commonly found in proteins. This standard set of twenty is the same throughout nature. Nucleic acid is made of polynucleotide chains. The repeating unit of the chain is a sugar (ribose for RNA , deoxyribose for DNA ) connected to a phosphate. A base is joined on to each sugar. There are four common bases in nucleic acid. DNA usually has adenine, guanine, cytosine and thymine. In RNA thymine is replaced by uracil.

Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 885-894 ◽  
Author(s):  
Leticia Rao ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Porcine Pepsin ◽  
Isolation And Characterization

The determination of the amino acid sequences of 70 peptides obtained from a thermoiytic digest of penicillopepsin (EC 3.4.23.7) is described. Fifty-six unique sequences ranging from 2 to 13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.

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