scholarly journals Monobasic Proteolytic Cleavage Site

2020 ◽  
Author(s):  
Keyword(s):  
Cleavage Site ◽  
Proteolytic Cleavage ◽  
Proteolytic Cleavage Site

scholarly journals Consequences of exclusive expression in vivo of kit-ligand lacking the major proteolytic cleavage site

1998 ◽  
Vol 95 (20) ◽  
pp. 11903-11908 ◽  
Author(s):  
Y. Tajima ◽  
M. A. S. Moore ◽  
V. Soares ◽  
M. Ono ◽  
H. Kissel ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Proteolytic Cleavage ◽  
Kit Ligand ◽  
Proteolytic Cleavage Site

scholarly journals Characterizing proteolytic cleavage site activity using bio-basis function neural networks

2003 ◽  
Vol 19 (14) ◽  
pp. 1741-1747 ◽  
Author(s):  
R. Thomson ◽  
T. C. Hodgman ◽  
Z. R. Yang ◽  
A. K. Doyle
Keyword(s):  
Neural Networks ◽  
Basis Function ◽  
Cleavage Site ◽  
Proteolytic Cleavage ◽  
Proteolytic Cleavage Site

scholarly journals Poikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion

Blood ◽  
1993 ◽  
Vol 82 (7) ◽  
pp. 2210-2215 ◽  
Author(s):  
PG Gallagher ◽  
WE Roberts ◽  
L Benoit ◽  
DW Speicher ◽  
SL Marchesi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cleavage Site ◽  
Proteolytic Cleavage ◽  
Single Amino Acid ◽  
Tryptic Digestion ◽  
Gene Encoding ◽  
Hereditary Elliptocytosis ◽  
Proteolytic Cleavage Site ◽  
Alpha Spectrin ◽  
Self Association

Abstract Hereditary elliptocytosis (HE) is a heterogeneous disorder of red blood cells frequently associated with abnormal limited tryptic digestion of the alpha I domain of spectrin and impaired spectrin dimer self- association. We studied two related individuals with poikilocytic hereditary elliptocytosis (HE) of different severity. Limited tryptic digestion of spectrin from these individuals showed the presence of a variant alpha I/50b Kd peptide at the expense of the normal alpha I/80 Kd peptide. Amino acid sequence analysis of the abnormal peptide showed that the proteolytic cleavage occurred after the arginine at position 470 of the alpha spectrin chain. Spectrin from these patients had an impaired ability to undergo self-association, as evidenced by increased amounts of spectrin dimers in 4 degrees C extracts of erythrocyte membrane from affected individuals. The polymerase chain reaction was used to study the DNA sequence of the alpha spectrin gene encoding the region of the alpha spectrin chain surrounding the abnormal proteolytic cleavage site. We detected the in-frame deletion of the trinucleotide CAT, encoding histidine 469, two amino acid residues to the N-terminal side of the abnormal proteolytic cleavage site between residues 470 and 471. Similar to many other defects of spectrin associated with HE, this deletion occurs in helix three of repeat 5 of the proposed triple helical model of spectrin repeats.

scholarly journals Poikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion

Blood ◽  
1993 ◽  
Vol 82 (7) ◽  
pp. 2210-2215 ◽  
Author(s):  
PG Gallagher ◽  
WE Roberts ◽  
L Benoit ◽  
DW Speicher ◽  
SL Marchesi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cleavage Site ◽  
Proteolytic Cleavage ◽  
Single Amino Acid ◽  
Tryptic Digestion ◽  
Gene Encoding ◽  
Hereditary Elliptocytosis ◽  
Proteolytic Cleavage Site ◽  
Alpha Spectrin ◽  
Self Association

Hereditary elliptocytosis (HE) is a heterogeneous disorder of red blood cells frequently associated with abnormal limited tryptic digestion of the alpha I domain of spectrin and impaired spectrin dimer self- association. We studied two related individuals with poikilocytic hereditary elliptocytosis (HE) of different severity. Limited tryptic digestion of spectrin from these individuals showed the presence of a variant alpha I/50b Kd peptide at the expense of the normal alpha I/80 Kd peptide. Amino acid sequence analysis of the abnormal peptide showed that the proteolytic cleavage occurred after the arginine at position 470 of the alpha spectrin chain. Spectrin from these patients had an impaired ability to undergo self-association, as evidenced by increased amounts of spectrin dimers in 4 degrees C extracts of erythrocyte membrane from affected individuals. The polymerase chain reaction was used to study the DNA sequence of the alpha spectrin gene encoding the region of the alpha spectrin chain surrounding the abnormal proteolytic cleavage site. We detected the in-frame deletion of the trinucleotide CAT, encoding histidine 469, two amino acid residues to the N-terminal side of the abnormal proteolytic cleavage site between residues 470 and 471. Similar to many other defects of spectrin associated with HE, this deletion occurs in helix three of repeat 5 of the proposed triple helical model of spectrin repeats.

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