Abstract: A transfection reagent and a method for enhancing transfection efficiency are described. A nucleic acid is provided, and a disaccharide is added as a transfection reagent. The disaccharide is composed of two identical monosaccharides. The transfection reagent is then applied to cells to introduce the nucleic acid into the cells.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: A fungal glucoamylase including a mutation pair Asn20Cys coupled with Ala27Cys forming a disulfide bond between the two members of the pair. The mutation provides increased thermal stability and reduced isomaltose formation to the enzyme. A fungal glucoamylase including a 311-314Loop mutation wherein reduced isomaltose formation is provided by the mutation is also provided. A fungal glucoamylase including a mutation Ser411Ala wherein increased pH optimum and reduced isomaltose formation is provided by the mutation is also provided. Combinations of the mutations in engineered glucoamylases are also provided as are combinations with other glucoamylase mutations that provide increased thermal stability, increased pH optimum and reduced isomaltose froamtion for cumulative improvements in the engineered glucoamylases. Also provided is a fungal glucoamylase including a mutation of Ser30Pro coupled with at least two stabilizing mutations forming a disulfide bond between the two stabilizing members.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation, The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: Non-naturally occurring mutant hemoglobins rHb (&bgr;N108Q) and rHb (&bgr;L105W) are provided that have a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. rHb (&bgr;N108Q) also exhibits enhanced stability against autoxidation. The mutant hemoglobins are preferably produced by recombinant DNA techniques. Such mutant hemoglobins may be used as a component of a blood substitute and hemoglobin therapeutics.

Abstract: The present invention relates to a method for recovery and purification of isoamylase by raw starch adsorption method. Various raw starches are used to recover the isoamylase produced by a bacterium such as Pseudomonas amyloderamosa. The method comprises using raw starch to adsorb isoamylase under conditions suitable for such adsorption and isolating the adsorbed enzyme. The isoamylase adsorption rate varied with the species of raw starch. Additionally, raw starch can be recycled.