1985
DOI: 10.1271/bbb1961.49.1985
|View full text |Cite
|
Sign up to set email alerts
|

Properties of a trypsin inhibitor from Job's-tears (Coix lacryma-jobi L. var. Ma-yuen Stapf).

Abstract: A heat stable trypsin inhibitor was found in the bran of soft-shelled job's-tears {Coix lacrymajobi L. var. Ma-yuenStapf) seeds. This inhibitor seemed to be a simple protein, and the molecular weight was about 12,000. Similar to other heat stable trypsin inhibitors, this inhibitor also contained manycysteine or cystine residues in the molecule. This inhibitor inhibited bovine trypsin at the molar ratio of 1 to 2, showing that it was double-headed. Its activity was stable against the change of pH at the range o… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2

Citation Types

1
3
0

Year Published

1988
1988
2012
2012

Publication Types

Select...
4
1

Relationship

1
4

Authors

Journals

citations
Cited by 6 publications
(4 citation statements)
references
References 2 publications
1
3
0
Order By: Relevance
“…3B). These observations agree with most of the BBI are stable to pH and heat, [16][17] and Kunitz type inhibitors are more sensitive to heat.…”
Section: Puriˆcation Of Inhibitorssupporting
confidence: 85%
“…3B). These observations agree with most of the BBI are stable to pH and heat, [16][17] and Kunitz type inhibitors are more sensitive to heat.…”
Section: Puriˆcation Of Inhibitorssupporting
confidence: 85%
“…These observations agree with the fact that most of the BBI type inhibitors are quite stable to pH and heat. 5,6,15) Inhibitory property All the inhibitors strongly inhibited trypsin (Fig. 3A).…”
Section: Puriˆcation Of Inhibitorsmentioning
confidence: 91%
“…3,4) The BBI family inhibitors have a molecular mass of 7 kDa or 14 kDa, and are characterized by the high contents of Cys residues and high stability to heat and extreme pHs. 5,6) They are called double-headed inhibitors, because they bind and inhibit two serine proteinases at two independent reactive sites. 7) In spite of the accumulating information regarding the primary structures of BBI family proteins, there was no report concerning BBI-family trypsin inhibitors from other sources than Leguminosae and Gramineae plants.…”
mentioning
confidence: 99%
“…A cystatin from Job's tears might strongly inhibit the proliferation of viruses. A trypsin inhibitor in Job's tears 16,17) has been found.…”
mentioning
confidence: 92%