Office Action 2: Notice of Allowance (2024-10-22)

CLAIMS:
Amendments to the Claims

Please amend Claims 2, 28, 32, 36 and 46-47.The Claim Listing below will replace all prior versions of the claims in the application:Claim Listing

1\. (Original) A method of measuring the activity of a FAMIN protein comprising;providing an isolated FAMIN protein; and
determining the adenosine deaminase activity, purine nucleoside phosphorylase activity and/or methylthioadenosine phosphorylase activity of the FAMIN protein.

2\. (Currently Amended) A method of screening for a compound that modulates the activity of a FAMIN protein comprising;determining the adenosine deaminase activity, purine nucleoside phosphorylase activity and/or methylthioadenosine phosphorylase activity of an isolated FAMIN protein in the presence and absence of a test compound,
wherein a difference in the adenosine deaminase activity, purine nucleoside phosphorylase activity and/or methylthioadenosine phosphorylase activity of the FAMIN protein in the presence relative to the absence of test compound is indicative that the test compound modulates the activity of the FAMIN protein .

3\. (Previously Presented) A method according to claim 2 wherein a decrease in the adenosine deaminase activity, purine nucleoside phosphorylase activity and/or methylthioadenosine phosphorylase activity of the FAMIN protein in the presence relative to the absence of test compound is indicative that the test compound is a FAMIN inhibitor.

4\. (Original) A method according to claim 2 wherein an increase in the adenosine deaminase activity, purine nucleoside phosphorylase activity and/or methylthioadenosine phosphorylase activity of the FAMIN protein in the presence relative to the absence of test compound is indicative that the test compound is a FAMIN potentiator.

5\. (Previously Presented) A method according to claim 1 wherein the purine nucleoside phosphorylase activity is an adenosine phosphorylase activity.

6\. (Previously Presented) A method according to claim 1 wherein the adenosine deaminase activity of the FAMIN protein is determined by measuring the conversion of an adenosine molecule into an inosine molecule in the presence of the FAMIN protein.

7\. (Original) A method according to claim 6 wherein the method comprises contacting the isolated FAMIN protein with adenosine nucleoside in a reaction solution; and determining the amount of adenosine nucleoside or inosine nucleoside in the reaction solution following said contacting.

8\. (Previously Presented) A method according to claim 6 wherein a decrease in the concentration of adenosine nucleoside or an increase in the concentration of inosine nucleoside in the reaction solution is indicative of adenosine deaminase activity.

9\. (Previously Presented) A method according to claim 6 wherein; (i) the adenosine molecule is adenosine and the inosine molecule is inosine; (ii) the adenosine molecule is deoxyadenosine and the inosine molecule is deoxyinosine (iii) the adenosine molecule is 2'- deoxyadenosine and the inosine molecule is 2'deoxyinosine; or (iv) the adenosine molecule is 5'-deoxyadenosine and the inosine molecule is 5'deoxyinosine.

10\. (Cancelled)

11\. (Cancelled)

12\. (Cancelled)

13\. (Previously Presented) A method according to claim 1 wherein the purine nucleoside phosphorylase activity of the FAMIN protein is determined by measuring the conversion of a

purine nucleoside into a nucleobase and a ribose-1-phosphate molecule in the presence of the FAMIN protein.

14\. (Original) A method according to claim 13 wherein the method comprises contacting the isolated FAMIN protein with a purine nucleoside in a reaction solution; and determining the amount of purine nucleoside; or purine nucleobase and/or ribose- 1-phosphate molecule in the reaction solution following said contacting.

15\. (Original) A method according to claim 14 wherein the reaction solution comprises inorganic phosphate.

16\. (Previously Presented) A method according to claim 13 wherein a decrease in the concentration of purine nucleoside or an increase in the concentration of purine nucleobase and/or ribose-1-phosphate molecule in the reaction solution is indicative of purine nucleoside phosphorylase activity.

17\. (Previously Presented) A method according to claim 1 wherein the purine nucleoside phosphorylase activity of the FAMIN protein is determined by measuring the conversion of a nucleobase and a ribose-1-phosphate molecule into a purine nucleoside in the presence of the FAMIN protein.

18\. (Original) A method according to claim 17 wherein the method comprises contacting the isolated FAMIN protein with a nucleobase and a ribose- 1-phosphate molecule in a reaction solution; and determining the amount of purine nucleoside; or purine nucleobase and/or ribose- 1- phosphate molecule in the reaction solution following said contacting.

19\. (Previously Presented) A method according to claim 17 wherein a decrease in the concentration of nucleobase and a ribose- 1-phospate molecule or an increase in the concentration of purine nucleoside in the reaction solution is indicative of purine nucleoside phosphorylase activity.

20\. (Previously Presented) A method according to claim 13 wherein (i) the purine nucleoside is guanosine, the purine nucleobase is guanine and the ribose-1- phosphate molecule is a-D-ribose-1-phosphate;
(ii) the purine nucleoside is adenosine, the purine nucleobase is adenine and the ribose-1- phosphate molecule is a-D-ribose-1-phosphate;
(iii) the purine nucleoside is 2'-deoxyadenosine, the purine nucleobase is adenine and the ribose- 1-phosphate molecule is 2' deoxy a-D-ribose-1-phosphate; or (iv) the purine nucleoside is 5'-deoxyadenosine, the purine nucleobase is adenine and the ribose- 1-phosphate molecule is 5' deoxy a-D-ribose-1-phosphate.

21\. (Cancelled)

22\. (Cancelled)

23\. (Cancelled)

24\. (Previously Presented) A method according to claim 13 wherein the purine nucleoside is an inosine molecule.

25\. (Previously Presented) A method according to claim 24 wherein;
(i) the inosine molecule is inosine, the purine nucleobase is hypoxanthine and the ribose-1- phosphate molecule is a-D-ribose-1-phosphate; or (ii) the inosine molecule is deoxyinosine; the purine nucleobase is hypoxanthine and the ribose- 1-phosphate molecule is 2'deoxy-a-D-ribose-1-phosphate.

26\. (Cancelled)

27\. (Previously Presented) A method according to claim 1 wherein the methylthioadenosine phosphorylase activity of the FAMIN protein is determined by measuring the conversion of methylthioadenosine into adenine and a methylthioribose-1-phosphate molecule in the presence of the FAMIN protein.

28\. (Currently Amended) A method according to claim 27 wherein the method comprises contacting the isolated FAMIN protein with a methylthioadenosine nucleoside in a reaction solution; and determining the amount of methylthioadenosine nucleoside \[\[; or\]\] z adenine nucleobase and/or methylthioribose-1-phosphate molecule in the reaction solution following said contacting.

29\. (Original) A method according to claim 28 wherein the reaction solution comprises inorganic phosphate.

30\. (Previously Presented) A method according to claim 28 wherein a decrease in the concentration of methylthioadenosine nucleoside or an increase in the concentration of adenine nucleobase and/or methylthioribose-1-phosphate molecule in the reaction solution is indicative of methylthioadenosine phosphorylase activity.

31\. (Previously Presented) A method according to claim 1 wherein the methylthioadenosine phosphorylase activity of the FAMIN protein is determined by measuring the conversion of adenine nucleobase and a methylthioribose-1-phosphate molecule into methylthioadenosine nucleoside in the presence of the FAMIN protein.

32\. (Currently Amended) A method according to claim 31 wherein the method comprises contacting the isolated FAMIN protein with adenine nucleobase and a methylthioribose-1- phosphate molecule in a reaction solution; and determining the amount of methylthioadenosine nucleoside \[\[; or\]\] adenine nucleobase and/or methylthioribose-1-phosphate molecule in the reaction solution following said contacting.

33\. (Previously Presented) A method according to claim 31 wherein a decrease in the concentration of adenine nucleobase and/or methylthioribose-1-phosphate molecule or an increase in the concentration of methylthioadenosine nucleoside in the reaction solution is indicative of methylthioadenosine phosphorylase activity.

34\. (Previously Presented) A method according to claim 27 wherein the methylthioadenosine nucleoside is 5-methylthioadenosine and the methylthioribose-1-phosphate molecule is S- methyl-5-thio-a-D-ribose- 1-phosphate.

35 (Previously Presented) A method according to claim 1 comprising determining the adenosine deaminase activity and purine nucleoside phosphorylase activity of the FAMIN molecule.

36\. (Currently Amended) A method according to claim 35 wherein the method comprising contacting the FAMIN protein with adenosine nucleoside in a reaction solution; and determining the amount of adenosine nucleoside \[\[or\]\] , hypoxanthine, and/or ribose-1-phosphate molecule in the reaction solution following said contacting.

37\. (Original) A method according to claim 36 wherein the reaction solution comprises inorganic phosphate.

38\. (Previously Presented) A method according to claim 36 wherein a decrease in the concentration of adenosine nucleoside or an increase in the concentration of hypoxanthine and/or ribose-1-phosphate molecule in the reaction solution is indicative of adenosine deaminase and purine nucleoside phosphorylase activity.

39\. (Previously Presented) A method according to claim 36 wherein (i) the adenosine nucleoside is adenosine and the ribose-1-phosphate molecule is a-D-ribose-1- phosphate;
(ii) the adenosine nucleoside is 2'-deoxyadenosine and the ribose-1-phosphate is 2'deoxy-a-D- ribose-1-phosphate; or (iii) the adenosine nucleoside is 5'-deoxyadenosine and the ribose-1-phosphate is 5' deoxy-a-D- ribose- 1-phosphate.

40\. (Cancelled)

41\. (Cancelled)

42\. (Previously Presented) A method according to claim 1 comprising determining the adenosine deaminase activity, purine nucleoside phosphorylase activity and methylthioadenosine phosphorylase activity of the FAMIN protein.

43\. (Previously Presented) A method according to claim 1 comprising determining the adenosine deaminase activity and the methylthioadenosine phosphorylase activity of the FAMIN protein.

44\. (Previously Presented) A method according to claim 1 comprising determining the purine nucleoside phosphorylase activity and the methylthioadenosine phosphorylase activity of the FAMIN protein.

45\. (Previously Presented) A method according to claim 1 wherein the FAMIN protein is human FAMIN.

46\. (Currently Amended) A method according to claim 45 wherein the FAMIN protein comprises an amino acid sequence having at least 80% identity to the sequence of amino acids 176-430of SEQ IDNO: 1.

47\. (Currently Amended) A method according to claim 45 wherein the FAMIN protein comprises an Ile residue or a Val residue at a position corresponding to position 254 of the amino acid sequence of \_SEQ ID NO: 1 \[\[)\]\].

48\. (Cancelled)

49\. (Previously Presented) A method according to claim 1 comprising identifying a test compound that inhibits FAMIN activity and optionally isolating and/or purifying the identified test compound.

OFFICE ACTION:
DETAILED ACTION
Notice of Pre-AIA  or AIA  Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Response to Amendment
The amendment received on 07/02/2024 is acknowledged.  Claims 2, 28, 32, 36 and 46-47 have been amended.
In light of the amendment to the claims the rejections under 35 U.S.C. 112(b) have been withdrawn, and the objection to claims 46-47 have been obviated.
Conclusion
Claims 1-9,13-20,24-25,27-39,42-47 and 49 are allowed.

APPLICANT REBUTTAL: REMARKS
Amendments to the Claims
Claims 2, 28, 32, 36 and 46-47 have been amended. Claim 2 has been amended to delete
"inhibitor." Support for the amendments is found, for example, in originally-filed claims 1 and 2.
Claims 28, 32 and 36 have been amended to delete "or." Support for the amendments is found,
for example, in originally-filed claims 28, 32 and 36, respectively. Claims 46-47 have been amended to remove the NP number. Support for the amendments is found, for example, in
originally-filed claim 47.
The amendments are made to expedite prosecution of this application. Applicant is not
conceding that the claims prior to amendment are not patentable. No inference should be made
that Applicant is disclaiming any subject matter of the present application, and Applicant
reserves the right to pursue the unamended claims or any other broader or narrower claims
supported by the disclosure at a later date, including in one or more continuing applications.
Cancellation of any claim herein is without prejudice to reinstatement in this or continuing
application.
No new matter has been added. Entry of the amendment to the claims is respectfully
requested.
Obj
ections
In the action, the limitation "NP 001121775.1" in claims 46 and 47 was deemed
allegedly objectionable. Solely to expedite prosecution, the claims have been amended to replace
the limitation with "SEQ ID NO: 1" in claims 46 and 47. Withdrawal of the objection is
respectfully requested.
Rej
ection Under 35 U.S.C.
&
In the action, previous claims 2-4, 28-30, 32 and 36-39 were alleged to be indefinite.
Solely to expedite prosecution, claim 2 has been amended to delete the term "inhibitor."
Claims 3-4 depend from claim 2 and contain the elements of the claim from which they depend.
Solely to expedite prosecution, claims 28, 32 and 36 have been amended to delete the
superfluous term "or." Claims 29-30 depend from claim 28, and claims 37-39 depend from claim
39, and contain the elements of the claim from which they depend.
Withdrawal of the rejections is respectfully requested.
Information Disclosure Statement
An Information Disclosure Statement (IDS) is being filed concurrently herewith. Entry
of the IDS is respectfully requested.
Payment of Fees
Authorization is hereby granted to charge the fees due with this submission, including
any extension of time fee, to Deposit Account No. 08-0380.
CONCLUSION