Please use this identifier to cite or link to this item: http://dlib.scu.ac.ir/handle/2027.42/24903
Title: A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins
Authors: Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA
Publisher: Elsevier
Description: A structural comparison between the A and B subunits of the five tetrameric Griffonia simplicifolia I isolectins (A4, A3B, A2B2, AB3, B4) was undertaken to determine the extent of homology between the subunits. The first 25 N-terminal amino acids of both A and B subunits were determined following the enzymatic removal of N-terminal pyroglutamate blocking groups with pyroglutamate aminopeptidase. Although 21 amino acids were common to both subunits, there were four unique amino acids in the N-terminal sequence of A and B. Residues 8, 9, 17, and 19 were asparagine, leucine, lysine, and asparagine in subunit A and threonine, phenylalanine, glutamic acid, and serine in subunit B. The last six C-terminal amino acids, released by digestion with carboxypeptidase Y, were the same for both subunits: Arg---(Phe, Val)---Leu---Thr---Ser---COOH. Subunit B, which contains one methionyl residue, was cleaved by cyanogen bromide into two fragments, a large (Mr = 31,000) and a small (Mr = 2700) polypeptide. Failure of the small fragment to undergo manual Edman degradation indicated an N-terminal blocking group, presumably pyroglutamate. Both subunits were digested with trypsin and the tryptic peptides were analyzed using reverse-phase HPLC. Tryptic glycopeptides were identified by labeling the carbohydrate moiety of the A and B subunit using sodium [3H] borohydride. Cysteine-containing tryptic peptides were similarly identified by using [1-14C]iodoacetamide. Approximately 30% of the tryptic peptides were common to both subunits. Thus, although the N- and C-terminal regions of A and B are similar, the subunits each possess unique sequences.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24903
More Information: Lamb, Jamie E., Goldstein, Irwin J. (1984/02/15)."A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins." Archives of Biochemistry and Biophysics 229(1): 15-26. <http://hdl.handle.net/2027.42/24903>
http://www.sciencedirect.com/science/article/B6WB5-4DW3DTS-1DX/2/ead7ee73573be001806ef22984a0aa5e
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6142693&dopt=citation
http://hdl.handle.net/2027.42/24903
6142693
http://dx.doi.org/10.1016/0003-9861(84)90125-5
Archives of Biochemistry and Biophysics
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Files in This Item:
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Title: A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins
Authors: Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA
Publisher: Elsevier
Description: A structural comparison between the A and B subunits of the five tetrameric Griffonia simplicifolia I isolectins (A4, A3B, A2B2, AB3, B4) was undertaken to determine the extent of homology between the subunits. The first 25 N-terminal amino acids of both A and B subunits were determined following the enzymatic removal of N-terminal pyroglutamate blocking groups with pyroglutamate aminopeptidase. Although 21 amino acids were common to both subunits, there were four unique amino acids in the N-terminal sequence of A and B. Residues 8, 9, 17, and 19 were asparagine, leucine, lysine, and asparagine in subunit A and threonine, phenylalanine, glutamic acid, and serine in subunit B. The last six C-terminal amino acids, released by digestion with carboxypeptidase Y, were the same for both subunits: Arg---(Phe, Val)---Leu---Thr---Ser---COOH. Subunit B, which contains one methionyl residue, was cleaved by cyanogen bromide into two fragments, a large (Mr = 31,000) and a small (Mr = 2700) polypeptide. Failure of the small fragment to undergo manual Edman degradation indicated an N-terminal blocking group, presumably pyroglutamate. Both subunits were digested with trypsin and the tryptic peptides were analyzed using reverse-phase HPLC. Tryptic glycopeptides were identified by labeling the carbohydrate moiety of the A and B subunit using sodium [3H] borohydride. Cysteine-containing tryptic peptides were similarly identified by using [1-14C]iodoacetamide. Approximately 30% of the tryptic peptides were common to both subunits. Thus, although the N- and C-terminal regions of A and B are similar, the subunits each possess unique sequences.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24903
More Information: Lamb, Jamie E., Goldstein, Irwin J. (1984/02/15)."A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins." Archives of Biochemistry and Biophysics 229(1): 15-26. <http://hdl.handle.net/2027.42/24903>
http://www.sciencedirect.com/science/article/B6WB5-4DW3DTS-1DX/2/ead7ee73573be001806ef22984a0aa5e
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6142693&dopt=citation
http://hdl.handle.net/2027.42/24903
6142693
http://dx.doi.org/10.1016/0003-9861(84)90125-5
Archives of Biochemistry and Biophysics
Appears in Collections:Research Collections

Files in This Item:
Click on the URI links for accessing contents.
Title: A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins
Authors: Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA;Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA
Publisher: Elsevier
Description: A structural comparison between the A and B subunits of the five tetrameric Griffonia simplicifolia I isolectins (A4, A3B, A2B2, AB3, B4) was undertaken to determine the extent of homology between the subunits. The first 25 N-terminal amino acids of both A and B subunits were determined following the enzymatic removal of N-terminal pyroglutamate blocking groups with pyroglutamate aminopeptidase. Although 21 amino acids were common to both subunits, there were four unique amino acids in the N-terminal sequence of A and B. Residues 8, 9, 17, and 19 were asparagine, leucine, lysine, and asparagine in subunit A and threonine, phenylalanine, glutamic acid, and serine in subunit B. The last six C-terminal amino acids, released by digestion with carboxypeptidase Y, were the same for both subunits: Arg---(Phe, Val)---Leu---Thr---Ser---COOH. Subunit B, which contains one methionyl residue, was cleaved by cyanogen bromide into two fragments, a large (Mr = 31,000) and a small (Mr = 2700) polypeptide. Failure of the small fragment to undergo manual Edman degradation indicated an N-terminal blocking group, presumably pyroglutamate. Both subunits were digested with trypsin and the tryptic peptides were analyzed using reverse-phase HPLC. Tryptic glycopeptides were identified by labeling the carbohydrate moiety of the A and B subunit using sodium [3H] borohydride. Cysteine-containing tryptic peptides were similarly identified by using [1-14C]iodoacetamide. Approximately 30% of the tryptic peptides were common to both subunits. Thus, although the N- and C-terminal regions of A and B are similar, the subunits each possess unique sequences.
URI: https://deepblue.lib.umich.edu/handle/2027.42/24903
More Information: Lamb, Jamie E., Goldstein, Irwin J. (1984/02/15)."A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins." Archives of Biochemistry and Biophysics 229(1): 15-26. <http://hdl.handle.net/2027.42/24903>
http://www.sciencedirect.com/science/article/B6WB5-4DW3DTS-1DX/2/ead7ee73573be001806ef22984a0aa5e
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6142693&dopt=citation
http://hdl.handle.net/2027.42/24903
6142693
http://dx.doi.org/10.1016/0003-9861(84)90125-5
Archives of Biochemistry and Biophysics
Appears in Collections:Research Collections

Files in This Item:
Click on the URI links for accessing contents.