Appeal No. 2005-0192 Page 2
Application No. 09/809,021
The examiner relies on the following references:
Altshuler 4,363,319 Dec. 14, 1982
Hanada et al. (Hanada) 5,945,103 Aug. 31, 1999
Lorne et al. (Lorne), “Transfusion Technology : Purification of Human Thrombin
by Affinity Chromatography For Its Use in Biological Glue Preparations,” Rev. Fr.
Transfus. Hemobiol., Vol. 32, pp. 391- 400 (1989)
Allary et al. (Allary), “Isolation by Affinity Chromatography, on Silica Support, of
Human Thrombin for Its Use in Biological Glue Preparations,” Annales
Pharmaceutiques Francaises, Vol. 48, No. 3, pp. 129-135 (1990)
Brezniak et al. (Brezniak), “High Stability of Dilute Human α-thrombin in Salt
Solutions,” Blood Coagulation and Fibrinolysis, Vol. 5, pp. 847-848 (1994)
Claims 18, 35, and 37 stand rejected under 35 U.S.C. § 102(b) as anticipated by
either Allary or Lorne.
Claims 18, 19, and 35-38 stand rejected under 35 U.S.C. § 103 as obvious in
view of either Allary or Lorne, combined with Hanada, Brezniak, and Altshuler.
We affirm.
Background
“Since it became possible to produce thrombin commercially, several
applications thereof have emerged. The main applications . . . are, besides diagnostic
purposes, the use as a local hemostatic or as a component of a tissue glue together
with a fibr[in]ogen-containing component.” Specification, paragraph [0002].1
“For formulation of the thrombin preparation as a component, which is stable and
storable in the liquid and, where appropriate, also in the frozen state, for use in a tissue
glue or on its own as a local hemostatic, a buffer should be used to adjust to a pH of
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