Single polypeptide detection using a translocon EXP2 nanopore

PROTEOMICS ◽  
2021 ◽  
pp. 2100070 ◽  
Author(s):  
Mitsuki Miyagi ◽  
Sotaro Takiguchi ◽  
Kazuaki Hakamada ◽  
Masafumi Yohda ◽  
Ryuji Kawano
Keyword(s):  
Single Polypeptide

scholarly journals Terminal deoxynucleotidyltransferase. Alignment of α- and β-subunits of the core enzyme along the primary translation product

1985 ◽  
Vol 227 (3) ◽  
pp. 1003-1007 ◽  
Author(s):  
C M Beach ◽  
S K Chan ◽  
T C Vanaman ◽  
M S Coleman
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Beta Subunits ◽  
Isolation And Purification ◽  
C Terminus ◽  
Human Lymphoblast ◽  
Catalytically Active ◽  
Single Polypeptide ◽  
Dna Nucleotide Sequence

Terminal deoxynucleotidyltransferase exists in multiple Mr forms, all apparently generated from a single polypeptide of 62kDa. On isolation and purification, the smallest catalytically active protein of this enzyme consists of two subunits, alpha (12kDa) and beta (30kDa). Recently a complementary-DNA nucleotide sequence has been reported for a portion of the enzyme from human lymphoblast. We have pinpointed the locations of the alpha- and beta-subunits within the elucidated nucleotide sequence. From these data, the portions of the nucleotide sequence coding for the catalytically important area of the transferase can be estimated. Here the amino acid sequence of a number of tryptic peptides from calf alpha- and beta-subunits is presented. Because of the striking homology between the amino acid sequence of the calf enzyme and that predicted for human lymphoblast enzyme, it is possible for us to conclude that the alpha-subunit was generated from the C-terminus of the precursor protein and the beta-subunit was non-overlapping and proximal.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres

N-Terminal amino acid sequence of rat tonin: homology with serine proteases

1978 ◽  
Vol 56 (9) ◽  
pp. 920-925 ◽  
Author(s):  
N. G. Seidah ◽  
R. Routhier ◽  
M. Caron ◽  
M. Chrétien ◽  
S. Demassieux ◽  
...  
Keyword(s):  
Serine Proteases ◽  
Terminal Sequence ◽  
Renin Substrate ◽  
Amino Terminal ◽  
Single Polypeptide Chain ◽  
Serine Protease Family ◽  
Terminal Amino ◽  
Single Polypeptide ◽  
Carboxy Terminal ◽  
Amino Terminal Sequence

In this paper, we present the amino-terminal sequence of rat tonin, an endopeptidase responsible for the conversion of angiotensinogen, the tetradecapeptide renin substrate, or angiotensin I to angiotensin II. It is shown that isoleucine and proline occupy the amino- and carboxy-terminal residues respectively. The N-terminal sequence analysis permitted the identification of 34 out of the first 40 residue s of the single polypeptide chain composed of 272 amino acids. The se results showed an extensive homology with the sequence of many serine proteases of the trypsin–chymotrypsin family. This information, coupled with the slow inhibition of tonin by diisopropylfluorophosphate, classified this enzyme as a selective endopeptidase of the active serine protease family.

scholarly journals Hepatic microsomal epoxide hydrase. Chemical evidence for a single polypeptide chain.

1979 ◽  
Vol 254 (14) ◽  
pp. 6240-6243 ◽  
Author(s):  
G C DuBois ◽  
E Appella ◽  
R Armstrong ◽  
W Levin ◽  
A Y Lu ◽  
...  
Keyword(s):  
Polypeptide Chain ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Chemical Evidence

scholarly journals Plant purple acid phosphatases - genes, structures and biological function.

2003 ◽  
Vol 50 (4) ◽  
pp. 1245-1256 ◽  
Author(s):  
Mariusz Olczak ◽  
Bronisława Morawiecka ◽  
Wiesław Watorek
Keyword(s):  
Disulfide Bridge ◽  
Acid Phosphatases ◽  
Amino Acid Residues ◽  
Disulfide Bridges ◽  
Inorganic Pyrophosphate ◽  
Manganese Ion ◽  
Substrate Preferences ◽  
Purple Acid Phosphatases ◽  
Single Polypeptide ◽  
Monomeric Proteins

The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this position and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pronounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.

scholarly journals Identification of Bovine Growth Hormone (BGH) Gene Polymorphism Using PCR-RFLP Method in Buffalo Bulls

2019 ◽  
pp. 1-8
Author(s):  
M. I. S. Hazlan Shah ◽  
M. S. Salisi ◽  
H. Wahid ◽  
M. S. Yahaya ◽  
Y. Rosnina ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Bubalus Bubalis ◽  
The Body ◽  
Bovine Growth Hormone ◽  
Agarose Gel ◽  
Single Polypeptide Chain ◽  
Pcr Rflp ◽  
Polymerase Chain ◽  
Single Polypeptide ◽  
Gland Development

Growth Hormone (GH) is a single polypeptide chain synthesised and secreted from anterior pituitary gland by somatroph cells. The product of GH gene hastens metabolism and promotes the growth of many organs and tissues especially bone, muscle and visceral organs. It also regulates growth, mammary gland development and lactation. Polymorphism in this gene is associated with increase in growth and development of many tissues in the body. Aim: The objective of this study was to investigate the polymorphism of bovine growth hormone (bGH) gene in buffalo bulls (Bubalus bubalis) using the PCR-RFLP (polymerase chain reaction–restriction fragment length polymorphism) technique. Design: Genomic DNA was extracted from a total of 10 bulls, consisting of Murrah – Swamp crossbred and pure Swamp buffalo bulls. A The 446 segment of the bGH gene was amplified. The DNA amplicons were detected in 2% agarose gel following 45 minutes of electrophoresis. They were thereafter digesting with AluI endonuclease restriction enzyme, and the digested DNA were detected in 2% agarose gel following electrophoresis for about 45minutes in all samples Results: Similar bands of approximately 300 and 146-bp each, with no variation, were detected in 2% agarose gel following electrophoresis in all the animals tested. Conclusion: Based on the Alu1 digestion result, all samples produced the same allele of the gene, with no polymorphism detected.

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