scholarly journals Partial Characterization of Immunoglobulin Cμ Gene of Water Buffalo (Bubalus bubalis) Predicts Distinct Structural Features of C1q-Binding Site in Cμ3 Domain

2013 ◽  
Vol 2013 ◽  
pp. 1-6
Author(s):  
Surinder S. Saini ◽  
N. K. Maiti ◽  
Azad K. Kaushik
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Water Buffalo ◽  
Helical Structure ◽  
Bubalus Bubalis ◽  
Structural Features ◽  
Partial Characterization ◽  
Protein Motif ◽  
High Amino Acid

Partial characterization of immunoglobulin Cµ gene of water buffalo (Bubalus bubalis) revealed high amino acid sequence identity with Cµ of cattle (94.28%) and sheep (91.71%). Four amino acid replacements (Met-301, Val-310, Asn-331, and Thr-432) in Cµ2, Cµ3, and Cµ4 of buffalo IgM are distinct, however. Unlike cattle, a codon deletion (GTG encoding valine at position 507 in cattle) and an insertion (GGC encoding glycine at position 532) occur in buffalo Cµ4. Three N-linked glycosylation (Asn-X-Thr/Ser) sites (one at position 325–327 in Cµ2; two at positions 372–374 and 394–396 in Cµ3) differentiate buffalo IgM from cattle and sheep. Similar to cattle, buffalo IgM has fewer prolines in Cµ2, which acts as hinge, which restricts Fab arm flexibility. Increased structural flexibility of the C1q-binding site in Cµ3 compensates for the rigid buffalo Cµ2 domain. Secondary structure of C1q-binding site is distinct in buffalo and cattle IgM where long alpha-helical structure is predominant that may be relevant to complement fixation function. Conserved protein motif “Thr-Cys-Thr-Val-Ala-His” provides protein signatures of C1q-binding region of ruminant species. The distinct structural features of C1q-binding site of buffalo and cattle IgM seem to be of functional significance and, therefore, useful in designing antibody based therapeutics.

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Dessy Natalia ◽  
Keni Vidilaseris ◽  
Pasjan Satrimafitrah ◽  
Wangsa Ismaya ◽  
Purkan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Saccharomycopsis Fibuligera ◽  
Sequence Identity ◽  
Ic50 Value ◽  
High Amino Acid ◽  
Ph Range

AbstractGlucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6–6.4 and at 50°C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 μM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.

Design, synthesis, and partial characterization of water-soluble .beta.-sheets stabilized by a dibenzofuran-based amino acid

1993 ◽  
Vol 115 (9) ◽  
pp. 3790-3791 ◽  
Author(s):  
Humberto Diaz ◽  
Kwok Yin Tsang ◽  
Danny Choo ◽  
Jose R. Espina ◽  
Jeffery W. Kelly
Keyword(s):  
Amino Acid ◽  
Beta Sheets ◽  
Water Soluble ◽  
Partial Characterization ◽  
Design Synthesis

scholarly journals Characterization of Amino Acid Substitutions in the Putative Binding Site of Bupropion in Glic

2020 ◽  
Vol 118 (3) ◽  
pp. 583a
Author(s):  
Dubem Onyejegbu ◽  
Jessica Shepherd ◽  
Elham Pirayesh ◽  
Akash Pandhare ◽  
Zackary R. Gallardo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Substitutions ◽  
Putative Binding Site

scholarly journals Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation

1994 ◽  
Vol 297 (2) ◽  
pp. 389-397 ◽  
Author(s):  
H U Simon ◽  
G B Mills ◽  
M Kozlowski ◽  
D Hogg ◽  
D Branch ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Amino Acid ◽  
Gene Product ◽  
Thymidine Incorporation ◽  
Structural Features ◽  
Nucleosome Assembly ◽  
Proliferating Cells ◽  
Amino Acid Similarity ◽  
Nucleosome Assembly Protein

We have isolated from a human thymus cDNA library a cDNA clone encoding a potential protein with 54% amino acid similarity to that encoded by a previously identified cDNA for yeast nucleosome assembly protein I (NAP-I). The deduced amino acid sequence for this newly identified cDNA, designated hNRP (human NAP-related protein), contains a potential seven-residue nuclear localization motif, three clusters of highly acidic residues and other structural features found in various proteins implicated in chromatin formation. When expressed as a fusion protein in Escherichia coli, hNRP reacted specifically with a monoclonal antibody raised against human NAP-I. The hNRP transcript was detected in all tissues and cell lines studied, but levels were somewhat increased in rapidly proliferating cells. Moreover, levels of both hNRP mRNA and protein increased rapidly in cultured T-lymphocytes induced to proliferate by incubation with phorbol ester and ionomycin. Phorbol 12-myristate 13-acetate/ionomycin-induced increases in both hNRP mRNA and mitogenesis, as measured by thymidine incorporation, were markedly inhibited, however, in cells treated with an hNRP antisense oligonucleotide. These results demonstrate a correlation between induction of hNRP expression and mitogenesis and taken together with the structural similarities between hNRP and yeast NAP-I suggest that the hNRP gene product participates in DNA replication and thereby plays an important role in the process of cell proliferation.

scholarly journals Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen

1987 ◽  
Vol 244 (2) ◽  
pp. 303-309 ◽  
Author(s):  
K Barnard ◽  
N D Light ◽  
T J Sims ◽  
A J Bailey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Partial Characterization ◽  
Cross Link ◽  
Cross Links

The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.

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