Temat: asparagine - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Asparagine slows down the decomposition of autophagic bodies in sugar starved embryo axes of lupin (Lupinus spp.)
Autorzy:: Borek, S.
Paluch, E.
Pukacka, S.
Powiązania:: https://bibliotekanauki.pl/articles/79839.pdf
Data publikacji:: 2013
Wydawca:: Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:: conference
asparagine
embryo
yellow lupin
Lupinus luteus
white lupin
Lupinus albus
Andean lupin
Lupinus mutabilis
sugar starvation
plasma membrane
phosphatidylcholine
Źródło:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Investigation of asparagine deamidation in a SOD1-based biosynthetic human insulin precursor by MALDI-TOF mass spectrometry
Autorzy:: Bierczyńska-Krzysik, Anna
Łopaciuk, Małgorzata
Pawlak-Morka, Renata
Stadnik, Dorota
Powiązania:: https://bibliotekanauki.pl/articles/1039302.pdf
Data publikacji:: 2014
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: asparagine deamidation
insulin precursor
superoxide dismutase
peptide mass fingerprinting
MALDI-TOF MS
Opis:: A biosynthetic human insulin precursor displayed enhanced susceptibility to deamidation at one particular site. The present study was undertaken to monitor progress of precursor deamidation at successive manufacturing stages. MALDI-TOF/TOF MS in combination with controlled endoproteinase Glu-C and endoproteinase Asp-N proteolysis was used for rapid and unambiguous determination of deamidated residue within the investigated structure. Close inspection of isotopic distribution patterns of peptides resulting from enzymatic digestion enabled determination of distinct precursor forms occurring during the production process. Asn, Asp, isoAsp and succinimide derivatives of the amino acid at position 26 were unambiguously identified. These modifications are related to the leader peptide of a precursor encompassing amino acid sequence corresponding to that of superoxide dismutase [Cu-Zn] (SOD1 1, EC=1.15.1.1). Monitoring of precursor deamidation process at successive manufacturing stages revealed that the protein folding stage was sufficient for a prominent replacement of asparagine by aspartic and isoaspartic acid and the deamidated human insulin precursor constituted the main manufactured product. Conversion proceeded through a succinimide intermediate. Significant deamidation is associated with the presence of SNG motif and confirms results achieved previously on model peptides. Our findings highlight an essential role of the specific amino acid sequence on accelerated rate of protein deamidation. To our knowledge, this is the first time that such a dramatic change in the relative abundance of Asp and isoAsp resulting from protein deamidation process is reported.
Źródło:: Acta Biochimica Polonica; 2014, 61, 2; 349-357
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Sequence analysis of enzymes with asparaginase activity.
Autorzy:: Borek, Dominika
Jaskólski, Mariusz
Powiązania:: https://bibliotekanauki.pl/articles/1044033.pdf
Data publikacji:: 2001
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: N-terminal nucleophile hydrolase
lysophospholipase
tRNA amidotransferase
aspartylglucosaminidase
asparaginase
L-asparagine
Opis:: Asparaginases catalyze the hydrolysis of asparagine to aspartic acid and ammonia. Enzymes with asparaginase activity play an important role both in the metabolism of all living organisms as well as in pharmacology. The main goal of this paper is to attempt a classification of all known enzymes with asparaginase activity, based on their amino acid sequences. Some possible phylogenetic consequences are also discussed using dendrograms and structural information derived from crystallographic studies.
Źródło:: Acta Biochimica Polonica; 2001, 48, 4; 893-902
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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