Abstract: A direct-type light source module including N-stage light sources and an optical sheet is provided. The optical sheet is disposed above the N-stage light sources, and an optical distance between the i-th-stage light source and the optical sheet is smaller than an optical distance between the i+1-th-stage light source and the optical sheet, where 1?i<N, and N is a positive integer greater than 1. A display device is also provided.

Abstract: A conveying device comprises a body in which a power source and two scroll wheels of the same diameter and rotating synchronously are disposed. Each scroll wheel is wound with an elongated elastic extension plate having rigidity, and one end of each elastic extension plate extends out of the body. When in use, the power source is used to drive the two scroll wheel to rotate synchronously, so as to drive the elastic extension plates of the two scroll wheels to synchronously extend out of or retract in the body. When the ends of the two elastic extension plates extended out of the body are assembled with a clamp or a loading seat, thereby, the conveying operation can be carried out.

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: 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.