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JournalISSN: 0002-1369

Agricultural and biological chemistry 

Oxford University Press
About: Agricultural and biological chemistry is an academic journal. The journal publishes majorly in the area(s): Amino acid & Isoelectric point. It has an ISSN identifier of 0002-1369. Over the lifetime, 13654 publications have been published receiving 182184 citations.


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Journal ArticleDOI
TL;DR: The transformation efficiency with Cs+ or Li+ was comparable with that of conventional protoplast methods for a plasmid containing ars1, although not for plasmids containing a 2 microns origin replication.
Abstract: When intact cells of Saccharomyces cerevisiae were treated with alkali cations or thiol compounds, the cells gained the ability to take up plasmid DNAs. The transformation efficiencies of yeast cells treated with alkali cations was greatly influenced by both the kind and concentration of cation used. The transformation efficiency also varied depending on the yeast strain. Polyethylene glycol was indispensable for the transformation. The uptake of plasmid DNAs into the yeast cells was found only in the presence of this polymer. Based on these results, the properties of transformation of intact yeast cells treated with alkali cations or thiol compounds were discussed.

3,091 citations

Journal ArticleDOI
TL;DR: A simple activity measurement of Lysozyme is described in this article, where the authors present a simple activity measurement of the enzyme and show that it is a simple molecule to measure.
Abstract: (1971). A Simple Activity Measurement of Lysozyme. Agricultural and Biological Chemistry: Vol. 35, No. 7, pp. 1154-1156.

690 citations

Journal ArticleDOI
TL;DR: In this article, both whipping and emulsifying properties of soybean products were investigated by using the commercial products in Japan, and they found that foam expansion and foam stability correlated positively with protein and negatively with fiber contents.
Abstract: Both whipping and emulsifying properties, the characteristic functional properties of soybean products, were investigated by using the commercial products in Japan. Whipping properties of the soybean products, expressed by foam expansion and foam stability, were found to correlate with water dispersible nitrogen, and the resultant foams were stable when the dissolved proteins were native. Thus, the native defatted soybean flour which contained native and soluble protein exhibited excellent whipping property. Emulsifying properties correlated positively with protein and negatively with fiber contents. As soybean protein isolate and soybean protein extract are rich in protein and poor in fiber contents, both of them show good emulsifying functions.

636 citations

Journal ArticleDOI
TL;DR: Several microorganisms capable of utilizing 1-aminocyclopropane-1-carboxylate (ACPC) were isolated from soil and it was suggested that this enzyme was a pyridoxal 5′-phosphate enzyme which has the molecular weight of 104000 and high specificity for ACPC.
Abstract: Several microorganisms capable of utilizing 1-aminocyclopropane-1-carboxylate (ACPC) were isolated from soil. A bacterium which belongs to Pseudomonas accumulated cellular α-aminobutyrate with consumption of ACPC and cells incubated with ACPC medium had the activity deaminating the substrate to form α-ketobutyrate. An enzyme, ACPC deaminase, was highly purified and its molecular weight, substrate specificity and absorption spectrum were investigated. These results suggested that this enzyme was a pyridoxal 5′-phosphate enzyme which has the molecular weight of 104000 and high specificity for ACPC, Km= 1.5 mM. A yeast, Hansenula saturnus, is also capable of forming ACPC deaminase, which has a lower molecular weight, 69000, and higher Km value, 2.6 mM.

610 citations

Journal ArticleDOI
TL;DR: The present enzyme requires no calcium ions for its activity, which clearly differs from known transglutaminases derived from mammalian organs, which have been defined as calcium-dependent enzymes.
Abstract: A microorganism producing transglutaminase was screened as an indication of hydroxamate- forming activity. The microbial transglutaminase was purified from the culture filtrate of the strain, S- 8112, which was supposed to belong to the genus Streptoverticillium. The molecular weight of the purified enzyme was found to be about 40,000 on SDS-polyacrylamide gel electrophoresis, the isoelectric point 8.9 and the optimal pH of the reaction 6~7. The present enzyme requires no calcium ions for its activity. Thus, it clearly differs from known transglutaminases derived from mammalian organs, which have been defined as calcium-dependent enzymes.

552 citations

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Performance
Metrics
No. of papers from the Journal in previous years
YearPapers
20149
20001
19982
1991642
1990673
1989646