Appeal No. 96-0352
Application 08/031,563
product defined by the patented claim. We find that the references of record do not support the
examiner’s contention that the claimed enzyme activity is necessarily and inevitably an inherent property
of the polymerized hemoglobin defined by the patented claim.
Hemoglobin is a complex molecule contained in red blood cells and is involved in the transport
of oxygen and carbon dioxide in the blood. The hemoglobin molecule has been described as consisting
of heme (a pigment of iron in the ferrous state) and globin (a protein formed of two alpha chains and
two beta chains having 141 and 146 amino acids respectively ). See Saunders at column 1, lines 36-
42. Oxygen combines rapidly and reversibly with hemoglobin to form oxyhemoglobin, and when the
iron of the hemoglobin molecule is oxidized to the ferric state, methemoglobin is formed. See Saunders
at column 1, lines 43-47. As acknowledged by the examiner in the answer at page 9 and as taught by
Saunders at column 1, lines 47 and 48, the enzyme, methemoglobin reductase, acts to reduce the
formed methemoglobin back to oxyhemoglobin. Scheinberg also confirms that the above reactions
take place and that methemoglobin reductase enzyme is present in red blood cells. See Scheinberg at
column 4, lines 22-31.
The examiner relies on the disclosure in the Sehgal patent at column 15, lines 53-59 as factual
support for his conclusion that the patented product inherently possesses the claimed enzyme activity.
This portion of the patent refers to a specifically exemplified polymerized hemoglobin product
produced by a complex and detailed process and indicates that the methemoglobin reductase activity in
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