A simple new technique of parallelizing methods for solving search problems which seek collisions in pseudorandom walks is presented. This technique can be adapted to a wide range of cryptanalytic problems which can be reduced to finding collisions. General constructions are given showing how to adapt the technique to finding discrete logarithms in cyclic groups, finding meaningful collisions in hash functions, and performing meet-in-the-middle attacks such as a known-plaintext attack on double encryption. The new technique greatly extends the reach of practical attacks, providing the most cost-effective means known to date for defeating: the small subgroup used in certain schemes based on discrete logarithms such as Schnorr, DSA, and elliptic curve cryptosystems; hash functions such as MD5, RIPEMD, SHA-1, MDC-2, and MDC-4; and double encryption and three-key triple encryption. The practical significance of the technique is illustrated by giving the design for three $10 million custom machines which could be built with current technology: one finds elliptic curve logarithms in GF(2155) thereby defeating a proposed elliptic curve cryptosystem in expected time 32 days, the second finds MD5 collisions in expected time 21 days, and the last recovers a double-DES key from two known plaintexts in expected time 4 years, which is four orders of magnitude faster than the conventional meet-in-the-middle attack on double-DES. Based on this attack, double-DES offers only 17 more bits of security than single-DES.
A 100-kDa protein that is a main component of the microsomal fraction from rabbit gastric mucosa is phosphorylated by cAMP-dependent protein kinase (PKA) in the presence of 0.2% Triton X-100. Microsomes from rabbit gastric mucosa possess activity of H,K-ATPase but not activity of Na,K-ATPase. Incubation of microsomes with 5 μM fluorescein 5′-isothiocyanate (FITC) results in both an inhibition of H,K-ATPase and labeling of a protein with an electrophoretic mobility corresponding to the mobility of the protein phosphorylated by PKA. The data suggest that the α-subunit of H,K-ATPase can be a potential target for PKA phosphorylation.