2002
DOI: 10.1016/s0196-9781(02)00098-0
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Isolation of cathepsin B inhibitory peptides, Cabin-A1 and -A2, from a tryptic and chymotryptic hydrolysate of human serum albumin

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Cited by 5 publications
(5 citation statements)
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“…Tryptic and chymotryptic digestion of HSA generated two peptides with cathepsin B inhibitory properties. These peptides corresponded to fragments 65-70 (SLHTLF; one letter code) and 403-407 (FQNAL) of HSA and named cabin-A1 and cabin-A2, respectively (Nakagomi et al 2002). The trypsin digest of HSA originated peptides with angiotensin converting enzyme (ACE) inhibition activity too.…”
Section: Serum Albumin Cryptidesmentioning
confidence: 99%
“…Tryptic and chymotryptic digestion of HSA generated two peptides with cathepsin B inhibitory properties. These peptides corresponded to fragments 65-70 (SLHTLF; one letter code) and 403-407 (FQNAL) of HSA and named cabin-A1 and cabin-A2, respectively (Nakagomi et al 2002). The trypsin digest of HSA originated peptides with angiotensin converting enzyme (ACE) inhibition activity too.…”
Section: Serum Albumin Cryptidesmentioning
confidence: 99%
“…Recently, the bioactivity of HA was studied using either the synthetic peptide or the HA purified by RP-HPLC from a 3-h tryptic hydrolysate of HSA at pH 8.4 (Nakagomi et al, 2002). The procedure for HA purification implies two successive chromatographic steps, after which, the fraction eluted from the HPLC column contains three different peptides, including HA.…”
Section: Specific Release Of Human Albutensin From Hsamentioning
confidence: 99%
“…HA was found in tryptic hydrolysates of HSA (Takahashi et al, 1998) and it was reported to show strong competitive ACE inhibition (Nakagomi et al, 2000). In recent work (Nakagomi et al, 2002), HA was found in the tryptic hydrolysate of HSA and the HPLC-purified peptide inhibited cathepsin B in vitro. For this reason, usage of HA in the development of anti-cathepsin B drugs has been suggested (Nakagomi et al, 2002).…”
Section: Introductionmentioning
confidence: 96%
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