scholarly journals Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal α-mannosidase B

1995 ◽  
Vol 305 (2) ◽  
pp. 363-366 ◽  
Author(s):  
C Emiliani ◽  
S Martino ◽  
J L Stirling ◽  
B Maras ◽  
A Orlacchio
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rapid Method ◽  
Protein Sequencing ◽  
Subunit Composition ◽  
Partial Sequence ◽  
Sequencing Analysis ◽  
Cloned Cdna

Human lysosomal alpha-mannosidase has been purified by a simple and rapid method in sufficient quantities for the analysis of its subunit composition and partial protein sequencing. Analysis of the N-terminal residues of the 30 kDa polypeptide has enabled us to confirm the identity of the recently cloned cDNA that was tentatively identified as that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Biochem. Biophys. Res. Commun. 200, 239-245] and to locate the position of this polypeptide within the total deduced amino acid sequence. This finding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.

scholarly journals Amino acid sequence and characterization of a protein inhibitor of protein kinase C.

1990 ◽  
Vol 265 (8) ◽  
pp. 4583-4591 ◽  
Author(s):  
J D Pearson ◽  
D B DeWald ◽  
W R Mathews ◽  
N M Mozier ◽  
H A Zürcher-Neely ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Protein Inhibitor ◽  
Kinase C

Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA

1987 ◽  
Vol 143 (2) ◽  
pp. 740-748 ◽  
Author(s):  
Micheline Misrahi ◽  
Michel Atger ◽  
Luc d'Auriol ◽  
Hugues Loosfelt ◽  
Cécile Meriel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Progesterone Receptor ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Cloned Cdna ◽  
Human Progesterone Receptor

scholarly journals Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits

2003 ◽  
Vol 15 (2) ◽  
pp. 119-122 ◽  
Author(s):  
Marli Lourdes de Oliveira ◽  
Leila Maria Beltramini ◽  
Salvatore Giovanni de Simone ◽  
Maria Helena Nasser Brumano ◽  
Rosemeire Aparecida Silva-Lucca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Amino Acid ◽  
Saline Extract ◽  
Hydrophobic Residues ◽  
Terminal Amino ◽  
Helix Conformation ◽  
Far Ultraviolet ◽  
Terminal Amino Acid Sequence

A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).

scholarly journals Characterization of two newly isolated Staphylococcus aureus bacteriophages from Japan belonging to the genus Silviavirus

2020 ◽  
Vol 165 (10) ◽  
pp. 2355-2359
Author(s):  
Naoya Kitamura ◽  
Eri Sasabe ◽  
Shigenobu Matsuzaki ◽  
Masanori Daibata ◽  
Tetsuya Yamamoto
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequences ◽  
Related Gene ◽  
Bacteriophage Therapy ◽  
Dna Rearrangements ◽  
Site Specific

Abstract Two Staphylococcus aureus bacteriophages, KSAP7 and KSAP11, were isolated from sewage and characterized. Based on morphology and DNA sequences, they were assigned to the genus Silviavirus, subfamily Twortvirinae, family Herelleviridae, whose members are hypothesized to be suitable for bacteriophage therapy. The KSAP7 and KSAP11 genomes were 137,950 and 138,307 bp in size, respectively. Although their DNA sequences were almost identical, evidence of site-specific DNA rearrangements was found in two regions. Changes in the number of PIEPEK amino acid sequence repeats encoded by orf10 and the insertion/deletion of a 541-bp sequence that includes a possible tail-related gene were identified.

scholarly journals Biochemical characterization of a second family of human Ia molecules, HLA-DS, equivalent to murine I-A subregion molecules.

1982 ◽  
Vol 156 (2) ◽  
pp. 550-566 ◽  
Author(s):  
S M Goyert ◽  
J E Shively ◽  
J Silver
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Amino Acid Sequence Homology ◽  
Molecular Weights ◽  
Hla Dr ◽  
D Region ◽  
Polypeptide Chains

In mice, two families of structurally distinct Ia molecules, one designated I-A and the other I-E, have been identified and characterized. The HLA-DR molecules represent one family of human Ia molecules equivalent to the murine I-E molecules on the basis of amino acid sequence homology. We describe the isolation and biochemical characterization of a second family of human Ia molecules, designated HLA-DS for second D-region locus, equivalent to the murine I-A molecules. The human HLA-DS molecules consist of two polypeptide chains, DS alpha (37,000 mol wt) and DS beta (29,000 mol wt), with 73% amino acid sequence identity to the murine I-A molecules. Furthermore, the HLA-DS molecules are closely linked genetically to HLA-DR molecules, a situation analogous to that observed in mice. The similarity in molecular weights of the DR and DS molecules might explain why others have failed to identify the latter in man.

Amino Acid Sequence and Characterization of a Nuclease (Nuclease Le3) fromLentinus edodes

2002 ◽  
Vol 66 (6) ◽  
pp. 1345-1355 ◽  
Author(s):  
Hiroko KOBAYASHI ◽  
Fumi KUMAGAI ◽  
Tadashi ITAGAKI ◽  
Takashi KOYAMA ◽  
Norio INOKUCHI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence

Characterization of Vitelline Membrane Outer Layer Protein I, VMO-I: Amino Acid Sequence and Structural Stability1

1995 ◽  
Vol 117 (6) ◽  
pp. 1183-1191 ◽  
Author(s):  
Shoko Kido ◽  
Yukio Doi ◽  
Fimi Kim ◽  
Emi Morishita ◽  
Hiroshi Narita ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Outer Layer ◽  
Vitelline Membrane
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