AMINO ACID COMPOSITIONS OF ALL THE TRYPTIC PEPTIDES FROM THE α AND β POLYPEPTIDE CHAINS OF ADULT HEMOGLOBIN OF THE SLOW LORIS (Nycticebus coucang)

2009 ◽  
Vol 4 (6) ◽  
pp. 405-413 ◽  
Author(s):  
Genji Matsuda ◽  
Tetsuo Maita ◽  
Bunji Watanabe ◽  
Hishiro Ota ◽  
Aiko Araya ◽  
...  
2009 ◽  
Vol 5 (6) ◽  
pp. 419-421 ◽  
Author(s):  
Genji Matsuda ◽  
Tetsuo Maita ◽  
Bunji Watanabe ◽  
Hisahiro Ota ◽  
Aiko Araya ◽  
...  

1967 ◽  
Vol 61 (2) ◽  
pp. 265-268 ◽  
Author(s):  
GENJI MATSUDA ◽  
TETSUO MAITA ◽  
NAGATOSHI IGAWA ◽  
HISAHIRO OTA ◽  
MASATO YAMAGUCHI

1978 ◽  
Vol 171 (3) ◽  
pp. 697-703 ◽  
Author(s):  
N A Panjwani ◽  
J J Harding

Tryptic peptides of citraconylated fragment alpha1-CB3 and chymotryptic peptides of fragment alpha1-CB3 of bovine corneal collagen were prepared, isolated and characterized. Their amino acid compositions were consistent with the amino acid sequence of fragment alpha1-CB3 from calf skin collagen. Two glycoside sites were identified in bovine corneal fragment alpha1-CB3, one of them being the first located in the overlap region of collagen. The results are related to the uniformly narrow collagen fibres found in cornea and essential for its transparency.


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