Imajoh S - Search Results

1

Separation of peptides on the basis of the difference in positive charge: simultaneous isolation of C-terminal and blocked N-terminal peptides from tryptic digests.

Kawasaki H, Imajoh S, Suzuki K. Kawasaki H, et al. Among authors: imajoh s. J Biochem. 1987 Aug;102(2):393-400. doi: 10.1093/oxfordjournals.jbchem.a122066. J Biochem. 1987. PMID: 3667575 Free article.

2

Fragmentation of an endogenous inhibitor upon complex formation with high- and low-Ca2+-requiring forms of calcium-activated neutral proteases.

Nakamura M, Inomata M, Imajoh S, Suzuki K, Kawashima S. Nakamura M, et al. Among authors: imajoh s. Biochemistry. 1989 Jan 24;28(2):449-55. doi: 10.1021/bi00428a007. Biochemistry. 1989. PMID: 2540798

3

Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.

Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K. Imajoh S, et al. Biochemistry. 1988 Oct 18;27(21):8122-8. doi: 10.1021/bi00421a022. Biochemistry. 1988. PMID: 2852952

4

The small subunits of calcium dependent proteases with different calcium sensitivities are identical.

Kawasaki H, Imajoh S, Kawashima S, Hayashi H, Suzuki K. Kawasaki H, et al. Among authors: imajoh s. J Biochem. 1986 May;99(5):1525-32. doi: 10.1093/oxfordjournals.jbchem.a135622. J Biochem. 1986. PMID: 3011775 Free article.

5

The COOH-terminal E-F hand structure of calcium-activated neutral protease (CANP) is important for the association of subunits and resulting proteolytic activity.

Imajoh S, Kawasaki H, Suzuki K. Imajoh S, et al. J Biochem. 1987 Feb;101(2):447-52. doi: 10.1093/oxfordjournals.jbchem.a121930. J Biochem. 1987. PMID: 3034871 Free article.

6

Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases.

Ishidoh K, Imajoh S, Emori Y, Ohno S, Kawasaki H, Minami Y, Kominami E, Katunuma N, Suzuki K. Ishidoh K, et al. Among authors: imajoh s. FEBS Lett. 1987 Dec 21;226(1):33-7. doi: 10.1016/0014-5793(87)80545-8. FEBS Lett. 1987. PMID: 3691815 Free article.

7

All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli.

Emori Y, Kawasaki H, Imajoh S, Minami Y, Suzuki K. Emori Y, et al. Among authors: imajoh s. J Biol Chem. 1988 Feb 15;263(5):2364-70. J Biol Chem. 1988. PMID: 2828366 Free article.

We have already determined the primary structure of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) from the cDNA sequence and revealed that the CANP inhibitor contains four internally repeating units which could be responsible for its multip …

We have already determined the primary structure of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) fr …

8

Regulation of activity of calcium activated neutral protease.

Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S. Suzuki K, et al. Among authors: imajoh s. Adv Enzyme Regul. 1988;27:153-69. doi: 10.1016/0065-2571(88)90015-5. Adv Enzyme Regul. 1988. PMID: 2854947

9

The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol.

Imajoh S, Kawasaki H, Suzuki K. Imajoh S, et al. J Biochem. 1986 Apr;99(4):1281-4. doi: 10.1093/oxfordjournals.jbchem.a135593. J Biochem. 1986. PMID: 3011770 Free article.

10

Limited autolysis of calcium-activated neutral protease (CANP): reduction of the Ca2+-requirement is due to the NH2-terminal processing of the large subunit.

Imajoh S, Kawasaki H, Suzuki K. Imajoh S, et al. J Biochem. 1986 Sep;100(3):633-42. doi: 10.1093/oxfordjournals.jbchem.a121755. J Biochem. 1986. PMID: 3023314 Free article.

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