Appeal No. 2002-2030 Page 2
Application No. 09/294,663
The examiner relies on the following reference:
Dandekar et al. (Dandekar), “Low levels of expression of wild type Bacillus
thuringienis var. kurstaki cryIA (c) sequences in transgenic walnut somatic
embryos,” Plant Science, Vol. 96, pp. 151-162 (1994)
Claims 1, 6, and 9 stand rejected under 35 U.S.C. § 112, first paragraph,
as nonenabled and inadequately described. We affirm and enter new a ground
of rejection of claims 3, 5-7, 9, 10, 21, and 22.
Background
“Vertebrate epithelial organs are covered . . . with a mucus lining, which
serves as a physical barrier between extracellular contents and the epithelial cell
surface. . . . The protective functions of the mucosal layer are largely dependent
upon heavily glycosylated proteins known as mucins.” Specification, page 1.
Several vertebrate mucin genes have been sequenced. Id., page 2. “Studies on
invertebrate mucins are very limited in comparison,” although several mucin-like
invertebrate proteins have been reported. Id.
The specification discloses an “intestinal insect mucin comprising two
nearly identical isoforms, IIM14 and IIM22, respectively. The proteins are
identical except for slightly different peptide length in some repetitive regions.”
Pages 3-4. “IIM” stands for “invertebrate intestinal mucin.” Id., page 6. Both
isoforms were cloned from Trichoplusia ni (cabbage looper) larvae. Id., page 4.
The IIM14 and IIM22 cDNAs encode 788 and 807 amino acids, respectively. Id.,
page 10. The specification provides a sequence analysis of the two T. ni IIM
isoforms. See pages 10-13.
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