What do you think about the THC percentage in modern flowers being allegedly higher than high quality hash of yesteryear?
What in the world was in that hash man... is that the famous Body hash where the natives run naked through the cannabis fields and later rub off the Hash LOFL !! 78% body rub and 23% THC in that hash LOL... joking, but wonder what constituted so much of the medium, maybe just a mix of plant biomass remaining from the processing procedure?
But, cannabis realistically cannot contain more than 30% THC as bio-mass.... cannot really measure thc on the plant though as it is an oxidized version of CBG-a or Olivetolic acid as pre cursor plant derivatives while they are living in expression
more on this plant thingy man
http://cannabisclinicians.org/wp-content/uploads/2012/07/OACIDinCanada.pdf
Quote from study
"
Δ
9
-Tetrahydrocannabinol (THC) and other cannabinoids are re-
sponsible for the psychoactive and medicinal properties of
Cannabis sativa
L. (marijuana). The
first intermediate in the cannabinoid
biosynthetic pathway is proposed to be olivetolic acid (OA), an
alkylresorcinolic acid that forms the polyketide nucleus of the can-
nabinoids. OA has been postulated to be synthesized by a type III
polyketide synthase (PKS) enzyme, but so far type III PKSs from
cannabis have been shown to produce catalytic byproducts in-
stead of OA. We analyzed the transcriptome of glandular tri-chomes from female cannabis
flowers, which are the primary site of cannabinoid biosynthesis, and searched for polyketide cy-
clase-like enzymes that could assist in OA cyclization. Here, we show that a type III PKS (tetraketide synthase) from cannabis tri-chomes requires the presence of a polyketide cyclase enzyme, oli-vetolic acid cyclase (OAC), which catalyzes a C2–C7 intramolecular aldol condensation with carboxylate retention to form OA. OAC is a dimeric
α
+
β
barrel (DABB) protein that is structurally similar to polyketide cyclases from Streptomyces
species.
OAC
transcript is present at high levels in glandular trichomes, an expression profile that parallels other cannabinoid pathway enzymes. Our identication of OAC both clarifies the cannabinoid pathway and demon-strates unexpected evolutionary parallels between polyketide
biosynthesis in plants and bacteria. In addition, the widespread oc-currence of DABB proteins in plants suggests that polyketide cyclases may play an overlooked role in generating plant chemical diversity. "