Abstract: A polypeptide represented by the following general formula (I): ##STR1## wherein X.sub.1 means a hydrogen atom, acetyl group of amino acid residue, X.sub.2 and X.sub.3 are either the same or different and mean individually an amino acid residue, and when X.sub.2 stands for Cys, X.sub.3 denotes an amino acid residue other than Cys.

Abstract: Glucose-6-phosphate dehydrogenase which is an enzyme for assaying creatinekinase for diagnolyzation of myocardial infraction is produced by culturing a transformant having DNA which codes amino acid sequence shown from its N-terminal in FIG. 1 and which is extraneous to a host to have genetic information of the DNA expressed and collecting glucose-6-phosphate dehydrogenase from the culture.

Abstract: The disclosure is made on a polydeoxyribonucleic acid having a base sequence encoding an amino acid sequence of a polypeptide which is a creatinase derived from a creatinase-producing microorganism belonging to the genus of Bacillus. The bsae sequence of the creatinase gene DNA and amino acid sequence of the creatinase have been clarified. The transformant having this polydeoxyribonucleic acid as well as a process for preparing the creatinase at a high productivity with the application of genetic engineering technique are disclosed.

Abstract: DNA having a base sequence encoding a specified amino acid sequence of a polypeptide constituting an L-.alpha.-glycerophosphate oxidase (GPO) is disclosed. A polypeptide having the specified amino acid sequence can be produced by inserting the DNA into a plasmid, culturing a transformant produced by introducing this plasmid into a host microorganism which is selected from microorganisms belonging to Escherichia coli, Bacillus subtilis, or Saccharomyces cerevisiae. The GPO is useful for the quantitative analysis of triglyceride, glycerine, etc., and the determination of lipase activity, when used in combination with other enzymes such as lipase, glycerol kinase, or the like, or with an ATP reagent.

Abstract: A polypeptide represented by the following general formula (I):X.sub.1 Ala Thr Lys Ala Val X.sub.2 Val Leu Lys Gly Asp Gly Pro Val Gln Gly Ile Ile Asn Phe Glu Gln Lys Glu Ser Asn Gly Pro Val Lys Val Trp Gly Ser Ile Lys Gly Leu Thr Glu Gly Leu His Gly Phe His Val His Glu Phe Gly Asp Asn Thr Ala Gly Cys Thr Ser Ala Gly Pro His Phe Asn Pro Leu Ser Arg Lys His Gly Gly Pro Lys Asp Glu Glu Arg His Val Gly Asp Leu Gly Asn Val Thr Ala Asp Lys Asp Gly Val Ala Asp Val Ser Ile Gle Asp Ser Val Ile Ser Leu Ser Gly Asp His X.sub.3 Ile Ile Gly Arg Thr Leu Val Val His Glu Lys Ala Asp Asp Leu Gly Lys Gly Gly Asn Glu Glu Ser Thr Lys Thr Gly Asn Ala Gly Ser Arg Leu Ala Cys Gly Val Ile Gly Ile Ala Gln (I)wherein X.sub.1 means a hydrogen atom, acetyl group or amino acid residue, X.sub.2 and X.sub.3 are either the same or different and mean individually an amino acid residue, and when X.sub.2 stands for Cys, X.sub.3 denotes an amino acid residue other than Cys.

Abstract: Antibiotic saccharocins of the formula ##STR1## wherein R is hydrogen (saccharocin) or hydroxyl (3'-oxysaccharocin) are produced by culturing a microorganism belonging to the genus Saccharopolyspora, for example Saccharopolyspora sp. AC 3440 FERM-P No. 6238, in a conventional nutrient medium, and separating the thus-produced saccharocins from the cultured medium. The noval saccharocins exhibit anti-bacterial activity against Gram negative bacteria.